Redox Properties of Electron Carrier Proteins

静岡大学教育学部研究報告 (自然科学篇

)第

46号 (1996.3)31‑48

Redox Properties of ^Electron Carrier Proteins

of Low Redox Potentials

Tatsuhiko Yecr

(Received for publication, October lt, lggs)

Abstract

This paper presents as many descriptions as possible on redox properties, ie, standard redox potentials, millimolar absorbances, and EPR-g values of various low-potential electron carrier ^proteins isolated from various sources. Some carrier proteins of high redox potentials and non-protein carriers are included for comparison.

1

. Introduction

Electron carrier proteins are playing important roles in the energy metabolism of various kinds of life forms, and some of them have been attracting attentions of a number of researchers. Each of these spot-lighted carrier proteins has been a subject

of more than ten papers. On the other hand, majority of carrier proteins appear

irregularly in various kinds of ^journals. This paper presents as many descriptions as possible on redox properties, ie, standard redox potentials, millimolar absorbances,

and EPR-€' values of various low-potential electron carrier proteins isolated from various sources. Some carrier proteins of high redox potentials and non-protein carri- ers are included for comparison, but these are fragmentary.

2. Tables

E is used instead of Eo ^(standard redox potential in mV). e is used instead of ^{I .nr}

(millimolar absorbance coefficient), and it refers to the value for the monomer in case

of proteins, unless otherwise specified; e552 means r .ru 8t bb2 nm, and for the oxidiz- ed form of the carrier unless indicated as r ^for the reduced form or as sq for the semiquinone form. A e is oxidized-minus-reduced millimolar absorbance difference at the wavelength specified. g _is EPR _5'-value for the oxidized carrier unless otherwise specified. 91, 92, ^etc correspond to the g-values which have the redox potentials of El,

F,2, etc, respectively. The number of amino acid residues (AA) _{per monomer is given}

with the PIR accession numbers (in _brackets) when available. References are cited by the name of the first author and the year of publication. The names of other authors are omitted. The abbreviations appearing in the tables are explained in the table, or self-explanatory.

2.1. Efecton Carrier Proteins 2.1.1. Monoheme cytochrome

Cytochrome c (C), cz (CZ>, c-550 (Cbb0), c-b53 (Cbb3), etc

C (horse) Heme,,/L04AA _[A0000s]

E:255 [Guo ^1991]

E:210 _[Guo 1991]

E:270 ^(pH 8.0) [Armstrong 1991J

Tatsuhiko Yagi

C,isoform‐ 1(Sα

ccん

α rO

ycθs caraυ^jsjα

a)Heme1/108AA[S22785]

E=260[Louie 1990]

Cl(Rん οαο

bαcι

ο r caps 滋ι s)Heme1/116AA[A25452]

E=358[Benning 1991]

Cl(Rん

ospjri″

じ脇 rabr 脇 )Heme1/112AA[S08213]

E=323[Salemme 1973]

C550(ゴ И ^jcrOの ノ

sι,s 

α arば _η

OSα

)Heme1/130AA

E=‐ 260[Cohn 1989]

C550(Parα θ ο

cc

Sル 滅ι

rttcα

ttS)Heme1/135AA E=250[Timko宙 ch 1974]

C551(Psc αο

ttο

πα s  αθ

rLttjんosα

)Heme1/′ 82AA E=260[Haladiian 1983]

E=260[Hi11 1987]

C553(Des

JJo脇iCrObj 脇 bαc Jαι れ

,9974,or DSM 1743)Heme1/mOl

E>‐ 50[Moura 1987]

C553(Dθ

s J」

o脇

jCrο bjじ脇 bαc Jαι 脇

Norway 4)Heme1/80AA E=50[Fauque 1979]

E=40[Bianco 1983]

C553(Das

J/ojjbriO dυs J/aricα

tts NCIMB 8372)Heme1/mOl E=0[Eng,Neuiahr 1989]

C553(Das

J/oυjbrjο

 dbs

J/aricα

tts NCIMB 8387,Berre‐ Eau)Heme1/mol

E>‐ 50[Moura 1987]

C553(Dθ

s JJoυjbrjο

  υ じ Jgatts Hildenborough)Heme1/79AA[A44752]

E=20[Bertrand 1982]

E=20[Bianco 1982]

E=20[Koller 1987]

E=62(pH 7.0,25° )[Verhagen 1994a]

gl=3.154,2.065[Bertrand 1982]

C553(Des

^{J」Oυ jb´}

jO υ

Jgα

ris Miyazaki)Heme1/79AA ECCDV5M]

E=26[Yagi 1994]

e695==0。8, e526==10。

1. e410==110, e360==28。

1, e280==19。

3, e553r==24.7, e524r==16.1,

e418r=154,e317r=33.1,Δ  e552=‐

^18。

0[Yagi 1994]

C553(Pθ

^Jο

dc″ ο

tt J

ι θο J閉 _)13.O kD E=220[Steinmetz Fischer 1982]

C555(Cん

^Jοrοbj 脇 ιん^jοs Jraιopん

jJ閉 )Heme1/′ 86AA[A00116]

E=145[Korszun 1977)

C555(Cん

JOrobjじ脇 υjbrjo」

orma)Heme1/11。 O kD E=80[Steinmetz 1983]

C555(Pθ JOdc″ οん

J

ι οο

J

m) E=160[Steinmetz 1982]

2.1.2. Polyhome cytochromo

El, E2, etc express the  Π lidpoint potentials of individual hemes(nlicroscopic potentials), and El, E2, etc fo1lowing superscriptm express the formal macroscopic potentials of polyheHlic cytochromes.

Cytochrome c3(C3)

C3(Des

J」obじJb

S CJongaι s)Heme4/′

^13。

7kD

El=‐ 30,E2,E3,E4(av)=‐ 165[Samain 1986]

e531=35。 6,e408=417,e280=31。 4,e551r=116.5,e522r=61。 4,e418r=718[Samain

1986]

C3(Des

J/o脇jCrο bj 脇 bαc 施ι れ

,9974;or DSM 1743)Heme4/mOl

El=¨ 70,E2=¨ 280,E3=¨ 300,E4=‐ 355[Moura 1988]

El=‐ 140,E2=… 200,E3=‐ 320,E4=‐ 360[Moren0 1991]

mEl=‐ 120,E2=‐ 286,E3=‐ 296,E4=¨ 335[Coutinh0 1994]

Redox Properties of Electron Carrier Proteins of Low Redox Potentials

³³

g1:2.99, 2.26, 1.51; g2:3.41; g3-3.05, 2.21, L.M; g4:3.18 [Moura ^1988]

C3 (Desulfomicrobiurn baculatunz Norway 4) Hemet,/ll8AA _ICCDVBN]

E1: -I25, E2:-L25, E3:-305, E4:-325 lCammack 19841

E1:-150, E2=-270, E3: -3%, E4:-355 [Gayda ^1985J

E1:-150, -275>82)-300, -325>E3)-330, -350>81)-SSS [Gayda ^1983]

El:-150, E2:-300, E3:-330, M:-355 [Guigliarelli ^1990]

'El:-165, E2:-305, E3:-365, E4:-400 [Bianco ^1981a]

-El: _{-L72, E2:-307, E3: -362, E4:-397 [Bianco 1981a]}

g1:2.94, 92:3.06, 93:3.01, g4:3.36 ^{[Cammack 19S4]}

g1-2.92; 92:3.37; g3:2.99; ^g4:3.L2 [Guigliarelli ^1990]

g1:2.936, 2.266, 1.510; g2:3.366, 1.985, 0.896); g3:3.006, 2.257,1.391;

g4:3.123, 2.L99, 1.358 [More ¹⁹⁹⁰⁾

e408: 570, e552r:130 A e552: -91 [Capeillene-Blandin ^1986]

C3 (Desulfouibrio desulfuricans Berre S) ^Heme n,/mol E1: -225, E2:-305, E3:-335, E4:-375 _[Bruschi 1984]

C3 (Desulfouibrio desulfuricans El Agheila Z) Hemen,/mol

E1: -235, E2:-265, E3: -290, M:-320 [Bruschi ^1984]

C3 (Desulfouibrio desulfuricans NCIMB 8372) Hemet,/mol

El: ^-%17, E2:-336, E3:-336, E4:-337 [Wang ^1991J E1: -250, E2:-313, E3:-333, E4:-398 [Wang ^1991J EI-: -255, E2:-323, E3: -325, E4:-395 [Wang ^1991J

El: ^-252, E2:-316, E3: -3L7, E4:-374 [Wang ^1991J

El: ^-252, E2:-3L7, E3: -3L7, E4:-363 [Wang ^1991J e553r:121 [Wang ^1991J

C3 (Desulfouibrio _{gigas NCIB 9332)} Hemeq,/lllAA ICCDVSG]

El: ^-235, E2:-235, E3:-306, B[:-315 _[Xavier 1979]

E1:-195, E2:-295, E3:-315, M:-330 [Nivi6re ^1988]

E1:-180, -225>EZ)-255, E3: ^-255, E4:-290 [santos ¹⁹⁸⁴ or Coletta 1991]

'E1: -205, E2:-290, _2g5>Eg)-80b, E4:_Ba0 (pH 9.9) [Coletta ^1gg1]

91-2.96, g2:2.83, g3:2.83, 94:2.96 [Xavier ^t979]

C3 (Desulfouibrio uulgaris Hildenborough) Hemer,/nl e,d, _[CCDV3]

El: -2U, E2:-310, E3:-319, M:-3%l lDerVartanian ^19?8]

E1: -226, E2:-34I, E3:-310, M:-377 [Niki ^1984]

E1: ^-290, E2:-335, E3:-345, M:-375 [Bruschi ^1984]

El:-300, E2:-320, E3:-350, B[:-365 [Teixeira ^1993]

'E1: -263, E2:-32L, E3: -329, E4:-381 [Niki ^1934]

'81: ^-250, E2:-310, E3:-310, E4:-330 [Dolla ^1994]

e408: ffi1 , e552r:159, A e552: -116 [Capeille,re-Blandin ^1986]

e552r:115 [Dolla ^1994]

C3 (Desulfouibrio uulgaris Miyazaki) Hemet,/

107

AA ICCDVBM]

E1,E2,E3,Bt(av) : -290 [Yagi ^19?1]

El: ^-243, E2:-316, E3: -299, M:-351 [Niki ^1984]

E1: -230, E2:-300, E3:-310, E4:-360 [Gayda ¹⁹⁸⁷¹

-220>El)-250, -320>EZ)-325, -330>Eg)-335, -355>M)-g0O lBenosman ^1989]

El: ^-270, E2:-325, E3:-305, M:-3bb ^(30", p'H 2.1) [Fan ^1gg0a]

'E1: -225, E2:-278, E3: _=298, M:-339 [Sokol ^1980]

-El: _-2/10, E2:-297, E3:-315, B[:-357 ^(pH 7.1) [Niki ^1984]

'El: ^-299, E2:-293, E3:-310, E4:-3S2 (p'H _{?.1) [Kimura} 1986]

'81: -227, E2:-287, E3: -320, M:-366 [Gayda ^1989J

'E1: -235, E2:-280, E3: -320, M:-370 [Benosman ^1989]

'81: ^-260, E2:-312, E3: -327, M:-369 [Fan ^1990b]

g1:2.72, t.675; 92:2.965, ^L.425; g3:3.38; g4:2.8L, 1.590 [Gayda ^1937]

g1:2.75; 92:2.97; g3:3.29; g4a:2.81 and g4b-2.93 [Benosman 1989]

g1: 2.790, 2.297, 1.638; 92:2.982, 2.3L2, 1.433; g3:3.405, 2.002, 1.069;

34

Tatsuhiko Yagi

g4a:2.946, 2.315, 1.516 [More ^1990]

e532:39.0, e4L0:4M, e350:90.8, e280:35.6, e552r:116, e524r:58.5, e4L9r:733, e325r:137, Ae552:-86.3 [Yagi ^1994]

CB (Desulfouibrio uulgaris Zhilina) _{E1: -t20,} ^Heme ',/mol

E2:-230, E3:-305, M:-325 [Bruschi ^19S4]

CB (Thermodesulfobacteriurn contrnune) ^Heme r,/ tg.gkO

El:-140, E2:E3:M:-Zg0 ^(pH 7.6, 25" ) [Hatcnikian ^1984]

e532: 48.5, e408.5:604, e351: 120, e551.5r: t30, e522.5r: 74.L, e418.5r: 975

[Hatctrikian ^19&4]

CB (Mr 26000) (Desulfomicrobiurn baculaturn Norway 4) Heme n,/tttA,A ^dimer E1:-180, E2:-210, E3: ^-320, M:-390 [Gayda ¹⁹⁸⁵¹

E1: ^-2L0, E2:-270, E3: -325, E4:-365 [Loutfi ^1989]

e553r: ?/12,/ dimer [Bruschi ^1994]

C3 (Mr 26000) (Desulfouibrio uulgaris Hildenborough) Hemet,/dimer

El: ^-290, E2:-335, E3: ^-345, E4:-375 [Loutfi ^1989]

C7 (Desulfuromonas acetoridans) Hemes,/ 68AA [CCDS7]

-L70>E1,E2,F;3> -220 [Bianco ^1981b]

E1: ^-L40, E2:-210, E3: ^-%10 lBruschi ¹⁹⁸⁴¹ High molecular mass cytochrome (Hmc)

Hmc (Desulfouibrio uulgaris Hildenborough) Heme,,./514AA _[439193]

16 hemes are classified into 3 groups, E:0, E:-100, E:-250 There are 1 or 2 high spin hemes (EPR). _[Bruschi 1992)

E1:61(n:1, high spin), E2:E16:-200(n:0.6) (pH 7.5) [Verhagen ^1994b]

Hmc (Desulfouibrio uulgaris Miyazaki) ^Heme ",/ ^AShD

El(high spin):60, E2:15, E3: E4:E5: E6: E7: -L20, E8: -I25, E9: -135, E10:

E11:-190, E12:813:-195, E14: -205, E15:816:-260 _[Ogata 1993]

e529:153, e409:1820, e355:380, e280:140, e553r:400, e523r:221, e4l9r:2735, e325r:630, Ae552:-286 [Yagi ^199aJ

2.1.3. Flavodoxin (Flx)

El is for Flx semiquinone,/dihydroFlx, and E2 is f.or Flx,/Flx semiquinone.

Flx (Anabaena uariabilis) tr'Utrl ,,/LIOAA,

E1:-890, E2:_f9b (pH ?.0), El:_419, EZ:-2S5 (pH _9.0) [Fittat ^1990]

Flx (Azacystis nidulani f'nnN r/tz0AA

El: ^-447 , ^{E2: -22L} lBntsch ^L9721

e580:0.1, e466:9.0, e400:4.8, e580sq:4.7, e466sq:2.6, e400sq:1.9, e580r:0, e466r:0.2 [Entsch ^1972]

Flx (Azotobacter chroococcum) FMN ,,/ mol

E1:-520, E2:-115-55x (pH-7.0) [Deistung ^1986J

e452:10.0, e370:9.0, e350:7.1, e506:e506sq:3.0, e358:e358sq:8.5, e580sq:5.2, e452sq:2.6, e370sq:5.2, e350sq:8.0, e417sq:e417r:1.8, e452r:1.6, e370r:5.5, e350r:5.4 [Deistung ^1986]

Flx I (Azotobacter uinelandit) FMN r,/Zt.SUO

El:-eZ0 ^(pH 7.0, ^25" ) [Klugkist ^1986]

e458:11.6, e599sq:4.8, e458sq:3.0, e458r:t.2 [Klugkist ^1986]

Flx II (Azotoflavin) (Azotobacter uinelandit) FMN

',/Lz9Ae, ^IFXAVEP]

El: ^-495, E2:50 (pH 8.2) [Barman ^L972]

E1: -4U, E2:-290 GH 7.7) [recalcd from Yoch L972a]

E1:_blb, E2:-ZS ^(pH 9.0, Zbo) [Watt lg7g]

El: ^{-480, E2: -22L} lHofstetter ¹⁹⁸⁵¹ El:-500 [Klugkist ^1986]

e452:11.3, e581sq: 53, 452sq: 3.0, e452r:1.5 [Klugkist ^1986]

Flx III (Azotobacter uinelandit) FMN,,/Zt.Skn

E1:-S00 (pH 7.0, 25" ) [Klugkist ^1986]

Redox Properties of Electron Carrier Proteins of Low Redox Potentials

³⁵

e46L- 10.6, e592sq: 5.4, e46lsq:3.1, e461r:1.5 [Klugkist ^1986]

Flx ^(C/o stridium beijerinchtt MP) FMN

',/tggnA, ^IFXCLEX]

El:-399, E2:-g2 (pH 7.0, ^25o ) ^{[Mayhew 1971]}

El:-480, E2:-162 (pH 8.2) [Mayhew ^1gZ1]

e575: 0.0, e445: 10.4, e376: 9.1, e272:46.8, e575sq: 4.62, eMSsq:Z.A, e376sq:4.85, e350sq: 8.4, e575r:0.0, eMSr:1.75 [Mayhew ^1971]

Flx (C/ostridium pasteurianum) FMN ,,/mol

El: ^-4L9, E2:-fg2 ^(pH 7.0, 25o ) [Mayhew ^1971]

El: ^-490, E2:-203 (pH 8.2) [Mayhew I97I]

e575:0.0, eM3:10.4, e374:8.47, e272:45.8, e575sq:4.55, e443sq: 2.08, e374sq: 4.65, e350sq: 8.4, e575r:0.0, eMBr:1.60 [Mayhew L97L]

Flx ^(De sulfouibrio El: ^-M0, E2:-150 ^gigas) fnaN [Dubourdieu ',/ ^{mol 1975]}

Flx (Desulfouibrio desulfuricans ATCC 27774) FMN,,/146AA E1:-387, E2:-aO (pH 6.7, ^25o ) ^{[Cataeira 1994]}

E1:-af0 ^(pH 7-10), E2:-100-59x(pH-8.0) [Caldeira ^L994]

e452:10.3, e275:37.0, e580sq: 4.2 lCaldeira ¹⁹⁹⁴¹ Flx ^(De sulfouibrio _e456: desulfuricans Berre-Eau) FttlN ',/ ^mol

10.04, e374:8.46, e274: 45.U [Fauque ^1987]

Flx ^(De sulfouibrio _{El:-aa0 (pH} salexigenes) FMN _{7-10), E2:-fo8} './ _(pH ^mol

6.7), -196 (pH 8.0) [Caldeira ^1994]

Flx (Desulfovibrio uulgaris Hildenborough) fUN

',/USA,A, IFXDV]

El: ^-M0, E2:-150 (pH 7.7) [Dubourdieu ^1975]

El: ^-462, E2:-175 (pH 8.2) [Dubourdieu ^1975]

El:-435, E2:-re9 ^(pH 7.0, pH-dependent 5.5-8.0) [curley ^1gg1]

El: -M0, E2:-f43 ^(pH 7.0, pH-dependent 5.5-8.0) [Curley ^1991]

e460: L0.7, e580sq: 4.L, e357r: 4.1 [Dubourdieu ^1975]

e458: 10.7, e378:13.0, e273: 46.3, e580sq:4.75 [Curley ^1991]

Flx (Escherichia coli) FMN r,/tzlA,A

El: ^{_455, E2:_Zgb (pH} Z.Z) lVetter ^1g?1]

El:-410, E2:-%0 (pH _7.7) [Vetter ^1g?1]

El: ^-440, E2:-279 (pH 8.2) lVetter ^1921]

Flx (Klebsiella pneurnoniae) FMN r,/tllA.A.

El: -4lz-Lgx (pH-7.0), E2: -lb8-Gbx (pH-?.0) [Deistung ¹⁹⁸⁶¹

e454:10.1, e370:9.6, e340:7.L, e502:e502sq:2.7, e352:e352sq:8.8, e580sq:4.1, e454sq:2.9, e370sq:5.9, e340sq:8.0, e410sq:e410r:2.4, e454r:1.3, e370r:4.3, e340r:4.9 _[Deistung 1986]

Flx (Megasphaera elsdenii; Peptostreptococcus elsdenii) FMN.,/L}7AA IFXME]

E1:-gZB (pH _7-10), E2:-11b-b9x(pH-2.0) [Mayhew ^1969]

2.1.4. lron-sulfur ^protein Ferredoxin (Fd)

Fd ^(Agr _E:-223, obacteriurn turnefaciens) g(red)=1.96 [van lZge-ZSl ^Beeumen ',/ ^{1975] mol}

Fd I (Azotobacter chroococcum) [3Fe- S]

,

[4Fe-4Sf ,,/ mol E1:-460 (alkaline), EZ:-6ab (pH 8.8) [Armstrong ^lgggJ e400: 29.8, e280:51.4 [Armstrong ^1983]

Fd I (Azotobacter uinelandii) [gFe-as],[4Fe-4s], ,/toee,e, IFEAV]

. ^{El:340, E2:-420, g:2.0L [sweeney 1975J}

E1: -425, E2:-647 [Iismaa ^1gg1]

Fd I ^(Bacillus polyrnyxa) _{[+f'e-aS] r,/g.gkO}

E: -390 [Yoch ^L972bJ

E: ^{-377 -11} x (pH-7.0) ⁽ⁿ - l, ^25" ) [stombaugh 19ZG]

Fd II ^{(Bacillus polymyra)}

Tatsuhiko Yagi

E=‐

422‐

24×

(pH‐

7.0)(n=1,25° )[Stombaugh 1976]

Fd(Bα

cjJJ s sι

θα

roι

ん arttopん

^jJじ

s)[4Fe‐ 4S]1/81AA[FEBSFF]

E=¨ 280(pH 8。 0)[Mullinger 1975]

Fd(働

rοttα

ι

^j

脇 υ

^jttOs

腕 D)[4Fe‐ 4S]2/82AA[FEKRV]

E=‐ 490(n=1)(pH 7.0)[Bachofen 1966]

E=‐ 489(n=2)(pH 9。

0‐

9.5)[Ke 1974]

E=‐

482‐11× (pH‐^8。

0)(n=1,25° )[Stombaugh 1976]

E=‐480(pH 8。

0,25°

)[Watt 1979]

E=‑470[Meyer 1983]

E=‐ 460(pH 8。

0,25°

)[Smith 1990]

Fd(CJο

sιrj醐

脇 α

cj醐^̲

月 cj)[4Fe‐ 4S]2/55AA[FECLCU]

E=‐ 434(n=1)(pH 7.0‐

7.9,25°

)[Stombaugh 1976]

E=‐

434¨

13×

(pH‐

7.0)(25° )[Lode 1976]

Fd(α

osι

rid 脇

^pαsι

θ

rjα

れじ屁 )[4Fe‐ 4S]2/55AA[FECLCP]

E=‐407[Sobel 1966]

E=‐ 390(n=1)(pH 6.1‐ 7.4)[Tagawa 1968]

El=‐ 367(n=1),E2=‐ 398(n=1)(pH 7.4)[EiSenstein 1969]

E=¨ 390(n=2)(pH 8。 8)[Ke 1974]

E=‐

403‐12× (pH‐

7.0)(n=1,25° )[Stombaugh 1976]

E=‐

405‐16× (pH‐

7.0)(25° )[Lode 1976]

E=‐

387‐11× (pH‐

7.0)(25°

_,0。

38M NaCl)[Lode 1976]

E=‐ 375(pH 8.0,25° )[Watt 1979]

E=‐ 370[Meyer 1983]

E=‐ 420(pH 7.6,lM NaCl)[Bianco 1984]

E=‐ 396(pH 6。

4‑8。7,25°

)ESmith 1990]

E=‐ 351(pH 7。 4)[Armstrong 1991]

e390=30[Sobel 1966]

Fd(CJosι

rう

醐 脇 ι

arι

α

rjυOrじ

脇 )[4Fe‐ 4S]2/55AA

E=‐424(n=1)(pH 7.0,25° )[Stombaugh 1976]

Fd I(CJosι rjdじ mι ん

arttο

α

cθ

ι

^jc

脇 )[4Fe‐

4S]1/′

63AA[FECLC]

El,E2(av)=‐ 350[Elliott 1982]

Fd H(CJο

^sι

rid 脇 ι ん ermο α

caιjc

れ )[4Fe¨ 4S]2/6.7kD(4Fe4S1/63AA?) El,E2(鉗 )=‐ 365,g=2.01;g(red)=2.05,1.92,1:89[Elliott 1982]

E=‐ 385(pH 8。

0,25°

)[Smith 1990]

e390=30。 4,e280=41.4 EElliott 1990]

Fd(CJosι河醐 脇 ι んarmoca″じ脇 )[4Fe‐ 4S]2/55AA[A24932]

E=‐ 430(pH 7.6,lM NaCl)[Bianco 1984]

e390=31.5[CapeilLtte¨ Blandin 1986]

Fd(α ostri醐 れ ι んθ rmosα

ccん

α ro″ ι

^jc

協 )[4Fe‐ 4S]2/55AA[FECLCT]

E=‐ 381(pH 7.0),E=‐ 408(pH 8。 0)(25° )[Smith 1990]

Fd I(Dθ

s J」

0腕

iC´

ο

bj

脇

bac

鯰ι屁 Norway 4)[4Fe‐ 4S]1/59AA[A25273]

E=‐374(pH 8.0)[Guerlesquin 1982]

E=‐ 375[Capeiltte̲Blandin 1986]

e390=17.5[Capeiltte̲Blandin 1986]

e400=17.5[Moura 1994]

Fd H(Des

J/0脇jCrObj 腕 bαc 施ι 脇

Norway 4)[4Fe¨ 4S]2/59AA[FEDV2N]

‐ 440>E>>¨ 500(pH 8。 0)[Guerlesquin 1982]

El=‐ 450,E2=‐ 500[Capeilltte‐ Blandin 1986]

E=‐ 550[Moura 1994]

e390=31.5[Capeilltte‐ Blandin 1986]

e400=31.6[Moura 1994]

Fd I(Das

J/oυjbrjο arricα屁

s Benghazi)[4Fe‐ 4S]1/61AA[FEDVlA],dimer

e380=21。 28,e30諄 =28.56,e283=37.87[Hatchikian 1979]

e400=28.5[Moura 1994]

Redox Properties of Electron Carrier Proteins of Low Redox Potentials

37

Fd II (Desutfouibrio africanus Benghazi) [afe-aS] ,,/A..SdD. dimer

e385:18.65, e308s:23.51, e290:28.95, e283:30.15 [Hatchikian ^19?9]

Fd III (Desulfouibrio africanus Benghazi) [gF'e-aS]'[aFe-as],,/unA IFEDV3A], dimer

El: ^-L40, E2:-410 [Moura ^1994]

e400:28.6 [Moura ^1994]

Fd [4Fe-4S]',/A.OUO (Desulfouibrio desulfuricans, Berre S, NCIB 3388)

E: -330 lZubieta ¹⁹⁷³¹

Fd I (Desulfouibrio grgas NCIB 9332) [af'e-aS] ,,/sga,A, IFEDVFG], ^dimer E:-330 ^(pH 7.6) [Bianco ^L9777

E: -455 [Moura ^19?8b]

E:-450 _[Moura 1994]

Fd II (Desulfouibrio grgas NCIB 9332) [gF'e-aS],,/sgAa, IFEDVFG], ^rerramer

E: -350 (pH 7.6) [Bianco ^L977]

E: -130 [Moura ^1978b]

El:-130, E2:-690 [Moreno ^1993]

E:-130 [Macedo ^1994]

Fd I (Desulfouibrio _uulgaris Miyazaki) [3Fe-aS],[aFe-4S],,/at/'d, [A300%], dimer E1>-300)nz (pH ?.4) [Ogata ^1988]

30>81>-310 (composite of 3 different Nernst curves), E2:-440 [Asso ^1995]

EI>-%5, E2:-425 [updated from Ogata 1988]

e400:31.5, e230:45.7 [updated from Ogata 19SS]

g1-2.01 ^(3Fe-4S), g}r:z.}M, 1.948, t.92A, 2.062 (af'e-AS) [Asso ^1995]

Fd II (Desulfouibrio uulgaris Miyazaki) [afe-aS] ,,/lgA,n IFEDV2V], ^dimer E:-405 ^(pH 7.4) [Okawara ^1988]

E: ^{-414 (pH 7.4)} [updated from Okawara ^1988]

E:-4L7 ^(pH 2.4, Zl") [Asso lggb]

e400:16.1, e280:31.0 lupdated from Okawara 1988]

S(red):2.0M, ^1.948, L.920; 2.062, 1.948, 1.898 [Asso ^1995]

Fd (Desulfurornonas acetoridans) [aFe-aS] r,/ ^6.ZUO e385: 29.8, e300*:37.3, e2.83:40.1 [Probst ^1978]

Fd (Giardia duodenalis) [gfe-aS] ,,/S.lg kD

e406:13.1, e296:16.65, g-Z [Townson ^1994]

F d ^(M ethano co ccus therrnolithotr ophicus) [4Fe-aS ] r,/

^AO

AA

I

S1M76 ] E=-385, g:2.0t ^(rough estimate) [Uatcnikian ^1989]

e390: 29, e283:36.7 [Hatchikian ^1989]

Fd (parsley) _E:-416 [2Fe-2S] _{(pH 7.9a),} './mol E:-gZ8 (pH 8.14) (ZS') _[Fee 1921]

Fd (Peptococcus aerogenes) _[4Fe-4S] z,/S+AA IFEPE]

E: ^-427-8 x (pH-7.0) (n: t, ^%o ) [stombaugh ^1976]

Fd III (Rhodobacter capsulatus) [Afe-aS] r,/L0OA,e, [A46701], dimer

81,E2,E3,M(av):-M0, 9:2.07, 1.91, 1.87; S(oxi) -L,/2 [Jouanneau ^1993]

e388:58.0, e450: 4L2, e388r :39.2, _{e450r: L6.9,/} dimer [Jouanneau ^1993]

Fd I (nhodoUacter capsulata) [aFe-aS] r,/1Se,A, [may ^{be A33498]}

E: -377(n:2) lZhu ¹⁹⁸²¹

Fd ^(spinach, Spinacia olarecea) lZfe-ZSlt,/97AA IFESPl or FESP2, not specified]

E:-41b(n:1) ^(pH G.?-8.2) [Tagawa ^1963]

E:_423(n:1) ^(pH 8.0-9.b) [Ke ^19Ta]

E:-48(n:1) ^(pH 2.0, 25") [stombaugh ^1gZ6J E:-430 ^(pH 8.0, 25") [Watt ^1929]

e465:8.80, e420:9.68, e325:L2.78, e276:20.16, e465r:3.70, e420r:4.55 [Tagawa

1e681

putidaredoxin (Pseudornonas putida) _[2Fe-2S] r,/ t}Ae,n IPXPSEP]

E:-230 [Meyer ^1983]

Tatsuhiko Yagi

High口 pOtential iron‐

sulfur proto:n(HiP:P)

HiPIP(Cん

rοttα

ι

^j

脇 υれ

Osじ

m)[4Fe‐ 4S]1/85AA EIHKREV]

E=350[Bartsch 1978]

E==360 [R/1eyer 1983]

e388=16.1,e283=41.3△ e480=10。 7[Bartsch 1978]

HiPIP(Cん

rοttα

ι

^j

腕 ″α

rttjれ

多ち DSM 173)[4Fe¨ 4S]i/8.9 kD E=355;pI=3.8,pI(red)=3.6[Wermter 1983]

HiPIP I(Ecι οι ん

^jorん

οαο

spjrα

  υα

c 01し

ι α )[4Fe‐ 4S]1/70AA[IHERl]

E=260[Meyer 1983]

HiPIP II(Ecι οι ん

^Jοrん

οご

ospjrα

  υα

c 01し

ι α )[4Fe‐ 4S]1/71AA[IHER2]

E==150 [Meyer 1983]

HiPIP I(Ecι οι ん

^jorん

οα

ospjrα

んα

Jopん^jJα

)[4Fe‐ 4S]1/70AA[IHERl]

E=120[Meyer 1983]

HiPIP II(Ecι οι ん

^jοrん

οdospjrα んα

Jopん^j施

)[4Fe‐ 4S]1/76AA[IHER2]

E=50[Meyer 1983]

HiPIP(Paracoccas species)[4Fe‐ 4S]1/8.lkD E=280[Bartsch 1978]

e385=14.8,e283=32.5△ e480=7.4[Bartsch 1978]

HiPIP(Rん ο dopsc αο οれα

s g̀Jα

ι

^jπosα

)[4Fe‐ 4S]1/74AA[IHRFG]

E=330[Bartsch 1978]

E==330 [Rtteyer 1983]

e388=15.3,e283=35.4△ e480=9.1[Bartsch 1978]

HiPIP(Rん οα

opsθ

ごο

ttο

れα s gJobiゎ rmJS)[4Fe‐ 4S]1/mol E=450[Meyer 1983]

HiPIP(Rん οご

ospjttr

れ ι οん θ 2761)[4Fe‐

4S]1/′

63AA?[IHQFT?]

E=330[Bartsch 1978]

E==330 [ltteyer 1983]

e385=16.9,e282=26.7△ e480=8.4[Bartsch 1978]

HiPIP(Rん _οα

ospjttr

脇 ι ο れθ 3761)[4Fe‑4S]1/63AA?[IHQFT?]

E=380[Meyer 1983]

HiPIP(7ん

^jο

capsα

 _praれ

れをだj)[4Fe‐ 4S]1/81AA[IHTF]

E=340[Bartsch 1978]

E==350 [Meyer 1983]

e375=15。 3,e283=45。 O  Δ  e480=8.5[Bartsch 1978]

Rubredox:n

Desulforedoxin(Des

J/Oυjbrjο

遷 誦実じ ^S)Fe2/′ 36AA[SDDVEG]

E=‐ 35,g=5。 73,7.72[Moura 1978a]

Rubredoxin I(Cん

Jοrοbj 脇 ιん^jοs Jraιoρん^jJ 腕

)Fe1/mol E=‑61[Meyer 1983]

Rubredoxin I((光

Jοrobjじ

屁 υ ^jbrjo/orれ a)Fe1/mol

peaks:575,492,370;pI=2.9[Steinmetz 1983]

Rubredo対 n II(Cん

JOrobj 胤 υ

jbrjo/ormθ

₎

peaks:575,492,370;pI=2.7[Steinmetz 1983]

Rubredo対 n(α

osι

rjd m pα

sι

θ

rjα

蔵 m)Fe1/54AA[RUCLEP,S2912o]

E=̲57[Lovenberg 1965]

Rubredoxin(Des

JJoυjbrjο arricα

れ ^s)Fel′

^/6。

OkD

e490=11。 45,e378=13.38,e355dl=12.28,e278=25.53[Hatchikian 1979]

Rubredoxin(Des

J/Oυjbrjο

 das

Jraだcαπs Berre‐

Eau)Fe1/′ 52AA

g=4.3,9。 4[Fauque 1987]

e491=6.98,e378=8.40,e278=18.52[Fauque 1987]

Rubredoxin(Desじ

J/oυJbrjο ♂むα

S NCIB 9332)Fe1/″ 52AA[RUDVEG]

E≡

^‐

40(pH 7.6),g=4.27,9。 4[Moreno 1993]

Rubredo対 n(Das

J/Oυjbrjο

 

υJgα

ris Miyazaki)Fe1/52AA[JX0241]

E=5[Shimizu 1989]

Redox Properties of Electron Carrier Proteins of Low Redox Potentials      39

e489=8.1,e280=18.2[Ogata 1994]

Rubredoxin(Des J/aromο πα S  α

Cθ

ι

Oκ^jα

α tts)Fe1/mol

e570轟

=2.6,e490=6.0,e370=7.1,e280=16.7[Probst 1978]

Rubredoxin(Psa ごοれοれα

S OJ00υ

ο

rα

tts)Fe2/′ 172AA[RUPSEO]

g=4.0[PetersOn 1966]

2.2. Non‐

protein electron carriers

2.2.1. N:cotinanlide nuclootido

NADtt       E=‐ 320,e259=18,e339r=6.22,e259r=15[Sober 1968]

NADPtt      E=‐ 324,e259=18,e339r=6.22,e259r=15[Sober 1968]

2.2.2. Flavin and quinone

E is for quinOne/quinOl(n=2),El is for semiquinone″ /quinol(n=1),and E2 is for

quinone/′ semiquinone(n=1).

9′10‐

Antraqu:nono(AQ)

AQ‑1‑sulfOnate       E=‐ 218(pH 7,25° )[Clark 1960]

AQ‑2‑sulfonate       E=‐ 226(pH 7,25° )[Clark 1960]

E=‐ 234(pH 7,30。 )[Clark 1960]

E=‐ 225(pH 7.4,25° )[van Beeumen 1975]

E=‐ 255[Xavier 1979]

AQ‐

1,5¨

disulfonate         E=‐ 174(pH 7,25° )[Clark 1960]

E=‐ 170(pH 7.4,25° )[van Beeumen 1975]

AQ‐

1,8¨

disulfonate         E=‐ 206(pH 7,25° )EClark 1960]

AQ‐

2,6‐

disulfonate         E=‐ 184(pH 7,25° )[Clark 1960]

AQ‐

2,7¨

disulfonate         E=‐ 182(pH 7,25° )[Clark 1960]

Flavins

FAD      E=‐ 219[Sober 1968]

El=‐ 124,E2=‐ 314[Anderson 1983]

e450=11.3,e375=9.3,e260=37[Sober 1968]

FMN       E=‐ 218[Clark 1960]

E=‐ 211[Sober 1968]

E=‐ 219(pH 7.1)[Sober 1968]

El=‐ 124,E2=¨ 314[Anderson 1983]

e450=12.2,e375=10。 4,e260=27.1[Sober 1968]

lumifla宙 n acetate         E=‐ 223[Wang 1991]

riboflavin      E=‐ 208[SOber 1968]

El=‐ 124,E2=ぃ 314[Anderson 1983]

e450=12.2,e375=10。 6,e260=27.7[Sober 1968]

1′4‐

Naphthoqu:none(NQ)′ menaquinone(MK)′ and v:tamin K(VK)

NQ      E=74[Wallenfels 1943]

E=64[Schnorf 1966]

E=58[Millazzo 1971]

E=84[Wagner 1974]

2‐

hydroxyNQ      E=‐ 145(pH 7.4,25° )[van Beeumen 1975]

2,3‐

dimethylNQ       E=‐ 80[Schnorf 1966]

3‐

heptaprenylNQ;demethylMK  E=36[Schnorf 1966;Holttnder 1976]

VKl(2‐ methyl¨

3‐

phytylNQ)   E=‐ 43[calcd frOm data of Riegel 1940]

E=‐ 80[McCawley 1940]

E=¨74[Sehnorf 1966]

E=‐ 78[Wagner 1974]

VK2 MK‐ 5(2‐ methyl‐

3‐αJJ‐ιrαtts¨

pentaprenylNQ)

E=‐ 108[Wagner 1974]

40

Tatsuhiko Yagi

VK z MK-6 (2-methyl-}- all-trans-hexaprenylNQ)

E: -67 [Wagner ^L974)

VK, MK-e (2-methyt-3-att-tr@ns-nonapreti#il?]rf

1e661

E:-70 [Wagner ^L974]

VKs (menadione; 2-methylNQ) E:-1 [schnorf ^1966]

2.2.3. Non-viologen artificial redox dye

dimethylphenosafranine E: -260 (pH _{1.0-12, 30"} ) [Clart ^1gG0]

indigomonosulfonate E: -157 (pH _1.1-11, 30o ) [Clart ^1gG0]

indigodisulfonate E:-125 (pH 1.1-11, 30o) [Clart ^1960]

E:-116 (pH 0.4-9, ^25o ) [Clart ^1960]

indigotrisulfonate E:-81 ^(pH 1.1-11, 30o) [Clart< ^1go0]

indigotetrasulfonate E: -46 (pH _1.1-11, 30o ) [Clart< ^1go0]

l-methoxyPMS E:63 ^(pH ?.0), e505:2.U, e386:15.9 [Hisada ^L977]

neutral red E: -325 (pH _2.1-11, B0o ) [clart< ^1960]

E:-329 (pH 0.5-t0, 25" ) [Chrn ^1960]

phenazine ethosulfate E:55 [Wang ^1991]

phenazine methosulfate (PMS) _{E:80 [Xavier} LgTg]

phenosafranine E: ^{-252 (pH} 1.1-11, 30o ) [clart< 1gG0]

E:-225 (pH ?.4, 25") [van Beeumen ^1975]

E=‑255[Xavier 1979]

E=¨ 245(pH 8。

0,25°

)[Watt 1979]

E=‐ 289[Wang 1991]

E=‐ 289(pH l.0‑12,30° )[Clark 1960]

E=‑289(pH 7。

4,25°

)[van Beeumen 1975]

tetraethylphenosafranine       E=‐ 254(pH 2.2‑9.8,30° )[Clark 1960]

tetramethylphenOsafranine    E="273(pH 3。

0‐8.2,30°

)[Clark 1960]

thiOindigodisulfonate      E=14(pH O.5‐

10.5,25°

)[Clark 1960]

thioindigotetrasulfonate         E=63(pH O‐

11.5,30°

)[Clark 1960]

toluidine blue       E=34(20° )[Clark 1960]

2.2.4.Viologen[abbre宙 ation;chemical name]

benzyl vi01ogen [BV; 1,1'‐

dibenzyl‐4,4'‐

dipyridinium dication]

E=‐ 359(pH indep,30° )[Michaelis 1933]

E=‐ 359(pH 8,30° )[Clark 1960]

E=‑354[Steckhan 1974]

E=‐ 311(pH 7.4,25° )[van Beeumen 1975]

E=‐ 345[Xavier 1979]

E=‐ 365(pH 8.0,25° )[Watt 1979]

E=‐ 360[Fraisse 1988]

E=‑350[Wang 1991]

e578r=12.0[Fraisse 1988]

e546r=9.75[Zoephel 1988]

betaine viologen [BtV; 1,1'‐ bis(carbOxymethyl)‐

4,4'‐

dipyridinium dicatiOn]

E=‐ 444(pH indep,30° )[Michaelis 1933]

E=̲444(pH ll,30° )[Clark 1960]

carbamoylmethyl vi010gen[CAV;1,1'¨ carbamoyl̲4,4'‐ dipyridiniuln dication]

E=‐ 296,e705r=2.2, e578r=14。4[Fraisse 1988]

6,7‐

dihydro‐

1,12‑dilnethyldipyrido[1,2‐ a:2,1‐

c]pyrazinium dibronlide E=‐ 580,e307=e310=15.6[Homer 1960a]

6,7‐

dihydro¨

2,11‐

dilnethyldipyridO[1,2‐

a:2,1‐

c]pyrazinium dibronlide E=‐ 349,e305=16.7[Homer 1960a]

E=‐ 490[Smith 1990]

safranine O

safranine T

Redox Properties of Electron Carrier Proteins of Low Redox Potentials ^4l

6,

7- dihydro ^{-3, 10-} dimethyldipyrido [ 1,2- a:Z,L - cTpy r azinium dibromide

E: -479, 19.8(e320:e330(20.6 [Homer ^1960a]

6,7-dihydrodipyridoh,2-a:2,1-cJpyrazinium dibromide

E:-548, e308:e311:19.0 [Homer ^1960a]

dimethyldiquat IDMDQ; 4,4'-dim ethyl-2,2'-dipyridino-1,1'-ethylenedication]

E:-514, e436r:6.1 [Fraisse ^1988]

dimethylpropyldiquat [DUfnq; ^4,4'-dim ethyl-2,2'-dipyridino-1,1'-propenyl dication]

E: -656 [Fraisse ^1988]

diquat [OQ; 1,1'-ethylene-2,2'-dipyridinium dication dibromide]

E:-350 [Homer 1960b; Zweig ^1965]

ethyl viologen [EV; 1,1'-diethyl-4,4' -dipyridinium dication]

E: -M9 (pH indep, 30o ) h,tictraelis ¹⁹³³¹

E: -M9 (pH 11, g0') _{[Clark 19G0]}

E:-480 [schwarfz ^Lg6l)

methyl viologen [MV; 1,1'-dimethyl-4,4'-dipyridinium dication; paraquatJ

E: -MG (pH indep, 30o ) [Uicnaefis ^1933]

E: -M0 (pH _8-13, 30o ) [Clart< ^1960]

E: ^-470 lZweig ¹⁹⁶⁵¹

E--444 (pH 7.a-11.0, 29") [Eisenstein ^1969]

E: -460 [Stombaugh ¹⁹⁷⁶¹

E:-M| ^{(pH 11.0)} [stombaugh ^1976]

E:-4b0 (pH 8.0, 25") [Watt ^L979]

E: -M9 (pH 7.0) [pltiott ^1982]

E: ^-444 [Fraisse ^1988]

E: -MG [Smith ^1990]

e396r: 42.6, e385r:2f1.4 lZweig ¹⁹⁶⁵¹ e600r: tL.4, 425r:1.6 [Eisenstein ^1969]

eb78r:g .6 lBadziong ¹⁹⁸⁰¹

e730r: 2.4, e578r:9.0 [Fraisse ^1988]

propyldiquat [eOq; ^2,2' -dipyridino-1,1'-propenyl dication]

E: -550, e492r:3.0 [Fraisse ^1988]

tetramethyl viologen [TMV; I,L',4,4'-tetramethyl-4,4'-dipyridinium dication]

E:-550, e?15r:1.2, e590r:9.7, e5?8r:8.7 [Fraisse ^1988]

1,1',3-trimethyl-4,4'-dipyridinium dication

E: -61? [Xavier ^1979]

triquat [TQ; 1,1'-trimethylene -2,2' -dipyridinium dication]

E: -550 [Homer ^1960b]

E:-&18 [steckhan L974]

E:-550, e387r:L4.0 LZweig ^1965J

3. Acknowledgements

The author is sincerely indebted to Mayumi Kuwahara who helped collecting papers,

and to Atsushi Yagi who rescued the collected data stored in a diskette which had been broken by an accident.

4. References

Anderson R F (fggg) Energetics of the one-electron reduction steps of riboflavin,

FMN and FAD to their fully reduced forms. Biochim Biophys Acta 772, L58-I62

Tatsuhiko Yagi

Armstrong FA, George SJ, Thomson AJ, Yates MG (1988) Direct electrochemistry in the characterization of redox proteins: Novel properties of Azotobacter 7Fe ferredoxin.

FEBS Lett 234, L07-Ll0

Armstrong FA, Bond AM, Hill HAO, Oliver BN, Psalti ISM ⁽¹⁹⁹¹⁾ Electrochemistry of cytochrome c, plastocyanin, and ferredoxin at edge- and basal-plane graphite electrodes interpreted via a model based on electron transfer at electroactive sites of microscopic dimentions in size. J Am Chem Soc 111, 9185-9189

Asso M, Mbarki O, Guigliarelli B, Yagi T, Bertrand P ⁽¹⁹⁹⁵⁾ EPR and redox characte-

rization of ferredoxins I and II from Desulfouibrio uulgaris Miyazaki. Biochem Biophys Res Commun zLI, L98-204

Bachofen R, Arnon Dl ⁽¹⁹⁶⁶⁾ Crystalline ferredoxin from the photosynthetic bacterium Chrornatium. Biochim Biophys Acta L20, 259-265

Badziong W, Thauer R K (1980) Vectorial electron transfer in Desulfouibrio uulgaris (Marburg) growing on hydrogen plus sulfate as sole energy source. Arch Microbiol L25, L67 -r74

Barman BG, Tollin G (L972) Flavin-protein interactions in flavoenzymes. Thermody- namics and kineties of reduction of Azotobacter flavodoxin. Biochemistry 11, 4755- 4759

Bartsch RG (1978) Purification of (afe-aS)'''' ferredoxins (high-potential iron-sulfur proteins) from bacteria. Methods Enzymol 53 329-U0 Chapter 35

Benning MM, Wesenberg G, Caffrey M S, Bartsch RG, Meyer TE, Cusanovich MA, Rayment l, Holden M (fggf) Uolecular structure of cytochrome cz isolated from Rhodobacter capsulatus determined at 2.5L resolution. J Mol Biol 220, 673-685

Benosman H, Asso M, Bertrand P, Yagi T, Gayda, J-P ⁽ 1989) ppn _study of the redox interactions in cytochrome cs from Desulfouibrio uulgaris Miyazaki. Eur J ^Bio-

chem 182, 51-55

Bertrand P, Bruschi M, Denis M, Gayda JP, Manca F ⁽¹⁹⁸²⁾ Cytochrome cess from Desulfouibrio uulgaris: Potentiometric characterization by optical and EPR studies.

Biochem Biophys Res Commun 106, ^756-760

Bianco P, Haladjian J ^(L977) Study of two forms of ferredoxin from Desulfouibrio grgas by differential pulse polarography. Biochem Biophys Res Commun 78, ^323-327

Bianco P, Haladjian J (fggfa) Current-potential responses for a tetrahemic protein:

A method of determining the individual half-wave potentials of cytochrome cs from Desulfouibrio desulfuricans strain Norway. Electrochim Acta 26, 1001-1004

Bianco P, Haladjian J ^(1981b) Electrode reaction of cytochrome ^cssr.s (cz) from Desul- furornonas acetoxidans. Bioelectrochem Bioenerg 8, 239-245

Bianco P, Haladjian J, Pilard R, Bruschi M ⁽¹⁹³²⁾ Electrochemistry of ^c-type

cytochromes. Electrode reactions of cytochrome csss from Desulfouibrio uulgaris Hildenborough. J Electroanal Chem L36, 29L-299

Bianco P, Haladjian J, Loutfi M, Bruschi M (1983) Comparative studies of monohemic bacterial c-type cytochromes. Redox and optical properties of. Desulfouibrio desulfuri- cans Norway cytochrom€

csss(s60>

and Pseudomonas aeruginoso cytochrome ^cur,. Biochem Biophys Res Commun 113, 526-530

Bianco P, Haladjian J, Tobiana G, Forget P, Bruschi M (19S4) Voltammetric determina-

tion of the redox potential of bacterial ferredoxins: Clostridium thermocellum ferredox-

in. Bioelectrochem Bioenerg 12, 509-516

Bruschi M, Loutfi M, Bianco P, Haladjian J ^(f984) Correlations studies between

structural and redox properties of cytochromes cs. ^Biochem Biophys Res Commun 120, 394-3gg

Bruschi M, Bertrand P, More C, Leroy G, Bonicel J, Haladjian J, Chottard G, Pollock WB R, Voordouw G ^{( 1992} ) Biochemical and spectroscopic characte fization of the

high molecular weight cytochrome c ^from Desulfouibrio uulgaris Hildenborough

expressed in Desulfouibrio desulfuricans G200. Biochemistry 31, ^3281-3288

Redox Properties of Electron Carrier Proteins of Low Redox Potentials

⁴³

Bruschi M ⁽¹⁹⁹⁴⁾ Cytochrome cg (Mr _{26000) isolated from} sulfate-reducing bacteria and its relationships to other polyhemic cytochromes from Desulfouibrio. Methods Enzymol 243, 140-155 Chapter 10

Caldeira J, Palma PN, Regalla M, Lampreia J, Calvete J, Scheifer W, LeGall J, Moura

l, Moura JJG (1994) _{Primary sequence,} oxidation-reduction potentials and tertiary- structure prediction of Desulfouibrio desulfuricans ATCC 27774 flavodoxin. Eur J Biochem 220, 987-995

Cammack R, Fauque G, Moura JJG, LeGall J ⁽¹⁹³⁴⁾ EPR studies of cytochrome

^cs

from Desulfouibrio desulfuricans strain Norway 4. Midpoint potentials of the four heams, and interactions with ferredoxin and colloidal sulphur. Biochim Biophys Acta 7U, 68-74

Capeillere-Blandin C, Guerlesquin F, Bruschi M (1986) Rapid kinetic studies of the electron-exchange reaction between cytochrorro ca and ferredoxin from Desulfouibrio desulfuricans Norway strain and their individtral reactions with dithionite. Biochim Biophys Acta 848, 279-293

Clark WM (1960) Oxidation-Reduction Potentials of Organic Systems. The Williams

& Wilkins, Baltimore

Cohn CL, Sprinkle JR, Alam J, Hermodson M, Meyer T, Krogmann DW (1989) _The amino acid sequence of low potential cytochrome

coso

from cyanobacterium Microcystis aeruginosa. Arch Biochem Biophys 270, 227-235

Coletta M, Catarino T, LeGall J, Xavier AV ^(fggf ) e thermodynamic model for the cooperative functional properties of the tetraheme cytochrome cs from Desulfouibrio grgas. Eur J Biochem 202, LL0I-1106

Coutinho lB, Xavier AV ⁽¹⁹⁹⁴⁾ Tetraheme cytochromes. Methods Enzymol 243, 119- 140 Chapter 9

Curley GP, Carr MC, O'Farrell PA, Mayhew SG (1991) _Redox properties of wild-type and mutant flavodoxins from Desulfouibrio uulgaris (HildenUorough). In: Flavins and Flavoproteins 1990, Proc 10th Int Symp, Como, Italy, July L5-20 (Curti B, Ronchi S,

Zanetti G, eds) , ^{Walter de} Gruyter, Berlin, pp 429-436

Deistung J, Thorneley RNF (1936) _Electron transfer to nitrogenase. Characterization of flavodoxin from Azotobacter chroococcutn, and comparison of its redox potentials with those of flavodoxins from Azotobacter uinelandii and Klebsiella pneun'Loniae @ifF- gene product). Biochem J 239, 69-75

DerVartanian DV, Xavier AV, Le Gall J ⁽¹⁹⁷⁸⁾ EPR determination of the oxidation- reduction potentials of the hemes in cytochrome cg from Desulfouibrio uulgaris.

Biochimie 60, ^32L-325

Dolla A, Florens L, Bianco P, Haladjian J, Voordouw G, Forest E, Wall J, Guerlesquin

F, Bruschi M ⁽¹⁹⁹⁴⁾ Characterization and oxidoreduction properties of cytochrome cs after heme axial ligand replacements. J Biol Chem 269, 6340-6346

Dubourdieu M, LeGall J, Favaudon V ⁽¹⁹⁷⁵⁾ Physicochemical properties of flavodoxin from Desulfouibrio uulgaris. Biochim Biophys Acta ^{376, 519-532}

Eisenstein KK, Wang JH ^{( fg6g} ) Conversion of light to chemical free energy.

I. Porphyrin-sensitized photoreduction of ferredoxin by glutathione. J ^{Biol Chem 744,}

L720-L728

Elfiott Jf, Ljungdahl LG (1982) Isolation and characterization of an Fer-S, ferredoxin (ferredoxin II) from Clostridium thermoaceticum. J Bacteriol 151, 328-333

Eng LH, Neujahr HY (1989) Purification and characterization of periplasmic C-type cytochromes from Desulfouibrio desulfuricans (NCnng $72>. Arch Microbiol 153, 60- 63

Entsch B, Smillie RM (1972) Oxidation-reduction properties of phytoflavin, a flavopro- tein from blue-green algae. Arch Biochem Biophys 151, 378-386

Fan K, Akutsu H, Kyogoku Y, Niki K ^(1990a) Estimation of microscopic redox poten-

tials of a tetraheme protein, cytochrome cs of Desulfouibrio uulgaris, Miyazaki F, and

partial assignments of heme groups. Biochemistry 29, 2257-2263

44

Tatsuhiko Yagi

Fan K, Akutsu H, Niki K, Higuchi N, Kyogoku Y (1990b) Determination of the macro- scopic formal potentials of cytochrom€ cs of. Desulfouibrio uulgaris, Miyazaki F, through the combined use of _'H NMR and an optically transparent thin-layer electrode cell.

J Electroanal Chem 278, 295-306

Fauque G, Bruschi M, Le Gall J (tgZg) Purification and some properties of cytochrome

csss(s'') isolated from Desulfouibrio desulfuricans Norway. Biochem Biophys Res Commun 86, 1020-t029

Fauque GD, Moura l, Moura JJG, Xavier AV, Galliano N, LeGall J ^{(1987) Isolation}

and characterization of a rubredoxin and a flavodoxin from Desulfouibrio desulfuricans Berre-Eau. FEBS Lett 2L5, 63-67

Fee AJ, Mayhew SG, Palmer G (1971) The oxidation-reduction potentials of parsley ferredoxin and its selenium-containing homolog. Biochim Biophys Acta fu45, 196-200

Fillat MF, Edmondson DE, Gomez-Moreno C (1990) Structural and chemical properties

of a flavodoxin from Anabaena PCC 7IL9. Biochim Biophys Acta 1040, 301-307

Fraisse L, Simon H ⁽¹⁹⁸³⁾ Observations on the reduction of non-activated carboxylates

by Clostridiurn formicoaceticum with carbon monoxide or formate and the influence

of various viologens. Arch Microbiol 150, 381-386

Gayda J-P, Bertrand P, More C, Guerlesquin F, Bruschi M ⁽¹⁹⁸⁵⁾ EPR potentiometric titration of c' type cytochromes. Biochim Biophys Acta 829, 262-267

Gayda JP, Yagi T, Benosman H, Bertrand P (1987) EPR redox study of cytochrome

ca from Desulfouibrio uulgaris Miyazaki. FEBS Lett 2L7, 57-6L

Gayda J-P, Benosman H, Bertrand P, More C, Asso M (1988) EPR determination of interaction redox potentials in a multiheme cytochrome: cytochrome cs from Desulfoui-

brio desulfuricans Norway. Eur J Biochem LlT, t99-206

Guerlesquin F, Moura JJG, Cammack R (1982) Iron-sulphur cluster composition and

redox properties of two ferredoxins from Desu,lfouibrio desulfuricans Norway strain.

Biochim Biophys Acta 679, 422-427

Guerlesquin F, Noailly M, Bruschi M (1985) Preliminary 'H-NMR ^studies of the inter- action between cytochrome cs and ferredoxin I ^from Desulfovibrio desulfuricans Nor-

way. Biochem Biophys Res Commun 130, 1102-1108

Guigliarelli B, Bertrand P, More C, Haser R, Gayda JP (1990) Singte-crystal electron paramagnetic resonance study of cytochrome cs from Desulfouibrio desulfuricans Nor- way strain. Assignment of the heme midpoint redox potentials. J Mol Biol 216, 161- 166

Guo LH, Hill HAO (1991) _Direct electrochemistry of proteins and enzymes. Adv Inorg Chem 36, 341-375

Haladjian J, ^Bianco P (1983) _Effect of pH on the electrochemical and spectrophoto- metric properties of Pseudornonas aeruginosa cytochrome cssri & comparison with horse

heart cytochrome c. Bioelectrochem Bioenerg 11, 319-326

Hatchikian EC, Jones HE, Bruschi M (1979) Isolation and characterization of a rubre- doxin and two ferredoxins from Desulfouibrio africanus. Biochim Biophys Acta 548, 47L-483

Hatchikian EC, Papavassiliou P, Bianco P, Haladjian J ^(t984) Characterization of cytochrorre cg from the thermophilic sulfate reducer Therm.odesulfobacterium cornrnune.

J Bacteriol 159, L040-1046

Hatchikian EC, Fardeau ML, Bruschi M, B6laich JP, Chapman A, Cammack R ⁽¹⁹⁸⁹⁾

Isolation, charactefization, and biological activity of the Methanococcus therrnolithotro- phicus ferredoxin. J Bacteriol 171, 23U-2390

Hill HAO, Page DJ, Walton NJ (198?) Direct electrochemistry of _hacterial cytochrome

cssr &t surface-modified gold electrodes. J Electroanal Chem 2I7, L29-140

Hisada R, Yagi T QSll) t-ltlethoxy-5-methylphenazinium methyl sulfate. A ^photo-

chemically stable electron mediator between NADH and various electron acceptors.

J Biochem 82, ^L469-L473

Redox Properties of Electron Carrier Proteins of Low Redox Potentials

45

Hofstetter W, DerVartanian DV ⁽ 1935) A ^modified flavodoxin with altered redox potentials is less efficient in electron transfer to nitrogenase. Biochem Biophys Res Commun L28, M\-Ug

HollSnder (fgZ6) Correlation of the function of demethylmenaquinone in ^bacterial

electron transport with its redox potential. _FEBS Lett ?2, ^98-100

Homer RF, Tomlinson TE ^(1960a) The stereochemistry of the bridged quaternary salts of. 2,2'-bipyridyl. J Chem Soc 2498-2503

Homer RF, Mees GC, Tomlinson TE (1960b) Mode of action of bipyridyl quaternary salts as herbicides. J Sci Food Agric 11, 309-315

fismaa SE, Vazquez AE, Jensen GM, Stephens PJ, Butt JN, Armstrong FA, Burgess

BK (1991) Site-directed mutagenesis of. Azotabacter uinelandii ferredoxin I. J ^Biol

Chem 266, 2I563-2157t

Jouanneau Y, Meyer C, Gaillard J, ^Forest E, Gagnon J ^(fg g) Purification and characterization of a novel dimeric ferredoxin (f'a m) from Rhodobacter capsulatus.

J Biol Chem 268, 10636-L0M4

Ke B, Bulen WA, Shaw ER, Breeze RH (L974) Determination of oxidation-reduction potentials by spectropolarimetric titration: Application to several iron-sulfur proteins.

Arch Biochem Biophys 162, 301-309

Kimura K, Nakajima S, Niki K, lnokuchi H (1985) Determination of formal potentials

of multihemoprotein, cytochrorl€ ca by 'H nuclear magnetic resonance. Bull Chem Soc

Japan 58, 1010-I0L2

Klugkist J, Voorberg J, Haaker H, Veeger C (1930) Characterization of three different flavodoxins from Azotobacter uinelandii. Eur J Biochem 155, 33-40

Koller KB, Hawkridge FM, Fauque G, LeGall J ⁽¹⁹⁸⁷⁾ Direct electron transfer reac-

tions of cytochrome cssg from Desulfouibrio uulgaris Hildenborough at indium oxide

electrodes. Biochem Biophys Res Commun t45, 6L9-624

Korzun ZR, Salemme FR (1977) Structure of cytochrorr€ csso of. Chlorobium thiosulfat- ophilum: primitive low-potentail cytochrome c. Proc Natl Acad Sci USA 74, 5244-5247

Lode ET, Murray CL, Rabinowitz JC (1976) _Apparent oxidation-reduction potential of. Clostridium acidi-urici ferredoxin. Effect of pH, ionic strength, and amino acid rep- lacements. J Biol Chem 251, ^1683-1687

Louie GV, Brayer GD (1990) _High resolution refinement of yeast iso-l cytochrome c and comparisons with other eucaryotic cytochromes c. J Mol Biol 2L4, 527-555

Loutfi M, Guerlesquin F, Bianco P, Haladjian J, Bruschi M ⁽¹⁹⁸⁹⁾ Comparative studies

of polyhemic cytochrome c isolated from Desulfouibrio uulgaris (Hildenborough) _and Desulfouibrio desulfuricans (Norway). _Biochem Biophys Res Commun L59, 670-676

Lovenberg W, Sobel BE (1965) Rubredoxin: A new electron transfer protein from Clostridium pasteurianum. Proc Natl Acad Sci USA 54, 193-199

McCawley EL, Gurchof C (1940) A mechanism of action for vitamin K. Univ Calif Pub Pharmacol 1, 325-338, CA 35: L466-67 (1941)

Macedo AL, Moura l, Surerus KK, Papaefthymiou V, Liu M-Y, LeGall J, Miinck E,

Moura JJG (1994) _{Thiol,/ disulfide formation} associated with the redox activity of the [Fe'Sr] cluster of Desulfouibrio gtgas ferredoxin II. J Biol Chem 269, 8052-8058

Mayhew SG, Foust GP, Massey V ⁽¹⁹⁶⁹⁾ Oxidation-reduction properties of flavodoxin from Peptostreptococcus elsdenii. J Biol Chem %4, 803-810

Mayhew SG (1971) Properties of two clostridial flavodoxins. Biochim Biophys Acta 235, 276-288

Meyer TE, Przysiecki, CT, Watkins JA, Bhattach aryya A, Simondsen RP, Cusanovich

MA, Tollin G (fgga) Correlation between rate constant for reduction and redox potential as a basis for systematic investigation of reaction mechanisms of electron

transfer proteins. Proc Natl Acad Sci USA 80, 6740-6744

Michaelis L, Hill ES (1933) tne ^viologen indicators. J Gen Physiol 16, 859-8Zg

Tatsuhiko Yagi

Millazzo G, Fiordiponti P, Menichini F, Piccioli A, Tasato ML, Vatteroni R ⁽¹⁹⁷¹⁾

Physico-chemical properties of some organic compounds of biological interest, II. In:

Biological Aspects of Electrochemistry (Millazzo G, Jones PE, Rampazzo L, ^eds )

,

Birkhause Verlag, Bazel, pp 463-475

More C, Gayda J P, Bertrand P (1990) Simulations of the g-strain broadening of low-spin hemoprotein EPR spectra based on the f'" hole model. J Magn Reson 90, 486-499

Moreno C, Campos A, Teixeira M, LeGall J, Montenegro Ml, Van Dijk C, Moura JJG

(fggf) Simulation of the electrochemical behavior of multiredox systems. Current potential studies on multi-hemes cytochromes. Eur J Biochem 202, 385-393

Moreno C, Franco R, Moura I, LeGall J, Moura JJG (1993) Voltammetric studies of the catalytic electron-transfer process between the Desulfouibrio gtgas hydrogenase and small proteins isolated from the same genus. Eur J Biochem 217, 981-989

Moura l, Xavier AV, Cammack R, Bruschi M, LeGall J ^(fgZ8a) A comparative spec-

troscopic study of two non-heme iron proteins lacking labile sulfide from Desulfouibrio grgas. Biochim Biophys Acta 533, 159-162

Moura JJG, Xavier AV, Hatchikian EC, LeGall J (1978b) Structural control of the

redox potentials and of the physiological activity by oligomerizaiion of ferredoxin.

FEBS Lett 89, Ll7-L79

Moura l, Fauque G, LeGall J, Xavier AV, Moura JJG (1987) Characterization of the cytochrome system of a nitrogen-fixing strain of a sulfate-reducing bacterium: Desul-

fouibrio desulfuricans strain Berre-Eau. Eur J Biochem L62, 547-5M

Moura l, Teixeira M, Huynh BH, LeGall J, Moura JJG (1983) Assignment of individual heme EPR signals of. Desulfouibrio baculatus (strain _{9974) tetraheme} cytochrome cs.

A redox equilibria study. Eur J Biochem 176, ^365-369

Moura JJG, Macedo AL, Palma PN (1994) Ferredoxins. Methods Enzymol ?t13, 165- 188 Chapter 12

Mullinger RN, Cammack R, Rao KK, Hall DO, Dickson DPE, Johnson CE, Rush JD, Simopoulos A ⁽¹⁹⁷⁵⁾ Physicochemical characterization of the four-iron-four-sulphide ferredoxin from Bacillus stearotherrnophilus. Biochem J 151, 75-83

Niki K, Kawasaki Y, Nishimura N, Higuchi Y, Yasuoka N, Kakudo M ⁽¹⁹⁸⁴⁾ Electro- chemical and structural studies of tetraheme proteins from Desulfouibrio - ^Standard

potentials of the redox sites and heme-heme interaction. J Electroanal Chem t68, 275-

286 ^'

Niviere V, Hatchikian EC, Bianco P, Haladjian J ⁽¹⁹⁸³⁾ Kinetics studies of electron

transfer between hydrogenase and cytochrome cs from Desulfouibrio gtgas. Electro- chemical properties of cytochrome cs. Biochim Biophys Acta 935, 34-40

Ogata M, Kondo S, Okawara N, Yagi T ⁽¹⁹⁸⁸⁾ Purification and characterization of ferredoxin from Desulfovibrio uulgaris Miyazaki. J Biochem 103, I2L-I25

Ogata M, Kiuchi N, Yagi T ⁽¹⁹⁹³⁾ Characterization and redox properties of ^high

molecular mass cytochrome cs (Hmc) _isolated from Desulfouibrio uulgaris Miyazaki.

Biochimie 75, 977-983

Okawara N, Ogata M, Yagi T, Wakabayashi S, Matsubara H (1988) Characterization and complete amino acid sequence of ferredoxin II from Desulfouibrio uulgaris Miyazaki.

Biochimie 70, 1815-1820

Peterson JA, Basu D, Coon MJ (1966) Enzymatic ar-oxidation. I. Electron carriers in fatty acid and hydrocarbon hydroxylation. J Biol Chem %lL, ^5L62-5L64

Probst

^f

, ^Moura JJG, Moura l, Bruschi M, LeGall J (1978) Isolation and characteriza-

tion of a rubredoxin and an ^(gF'e-SS) ferredoxin from Desulfuroftronas acetoxidans.

Biochim Biophys Acta 502, 38-M

Riegel B, Smith PG, Schweitzer CE (1940) _The oxidation-reduction potential of vitamin K

r

. J Amer Chem Soc 62, 992

Salemme FR,, Freer ST, Xuong NH, Alden RA, Kraut J ⁽¹⁹⁷³⁾ The structure of oxidiz-

ed cytochrome cz of Rhodospirillum rubrum. J Biol Chem 248, 3910 -392L

Redox Properties of Electron Carrier ^Proteins of Low Redox Potentials

⁴⁷

Samain E, Albagnac G, LeGall J ⁽¹⁹⁸⁶⁾ Redox studies of the tetraheme cytochrome

cs isolated from propionate-oxidizing, sulfate-reducing bacterium Desulfobulbus elongatus.

FEBS Lett 204, 247-250

Santos H, Moura JJG, Moura l, LeGall J, Xavier AV (1984) NMR studies of electron

transfer mechanisms in a protein with interacting redox centres: Desulfouibrio gtgas cytochrom€ cs. Eur J Biochem I4L, ^287-296

Schnorf U ⁽¹⁹⁶⁶⁾ PhD Thesis, cited in [Wissenbach ^1990].

Schwartz WM ⁽¹⁹⁶¹⁾ PhD Thesis, Univ of Wisconsin-Madison

Shimizu F, Ogata M, Yagi T, Wakabayashi S, Matsubara H ^{( fggg} ) ^{Amino acid}

sequence and function of rubredoxin from Desulfouibrio uulgaris Miyazaki. Biochimie 7T, LLTL-TL?7

Smith ET, Feinberg BA (1990) Redox properties of several bacterial ferredoxins using square wave voltammetry. J Biol Chem 265, t437L-L4376

Sobef BE, Lovenberg W (1966) Characteristics of. Clostridiurn pasteurianurn ferredoxin

in oxidation-reduction reactions. Biochemistry 5, 6-13

Sober HA ed. (1968) _Handbook of Biochemistry. The Chemical Rubber Co. Cleveland, Ohio

Sokol WF, Evans DH, Niki K, Yagi T ⁽¹⁹⁸⁰⁾ Reversible voltammetric response for a molecule containing four non-equivalent redox sites with application to cytochrome

cs

of. Desulfouibrio uulgaris, strain Miyazaki. J Electroanal Chem 108, 107-115

Steckhan E, Kuwana T ⁽¹⁹⁷⁴⁾ Spectroelectrochemical study of mediators. I. Bipyridy- lium salts and their electron transfer rates to cytochrome c. ^Ber Bunsenges Phys Chem 78, ^253-259

Steinmetz MA, Fischer U (1982) Cytochromes, rubredoxin, and sulfur metabolism of the non-thiosulfate-utilizing green sulfur bacterium Pelodictyon luteolum. Arch Microbiol L32, 204-2L0

Steinmetz MA, Tr[iper HG, Fischer U (1983) Cytochrome c-555 and iron-sulfur-proteins

of the non-thiosulfate-utilizing green sulfur bacterium Chlorobiurn uibrioform,e. Arch Microbiol 135, 186-190

Stombaugh NA, Sundquist JE, Burris RH, Orme-Johnson WH ^{( fgZ6} ) ^Oxiaation-

reduction properties of several low potential iron-sulfur proteins and of methylviologen.

Biochemistry 15, 2633-2UL

Sweeney WV, Ra binowitz JC, Yoch DC ^{( fgZS} ) ^{Hign and low reduction potential}

4Fe-4S x clusters in Azotobacter uinelandii GFe-AS' ), ferredoxin I. J Biol Chem 250, 7U2-7Ut

Tagawa K, Arnon Dl (fg68) O*iaation-reduction potentials and stoichiometry of electron transfer in ferredoxins. Biochim Biophys Acta 153, 602-613

Teixeira M, Campos JP (1993) cited in [Coutinho ^19%]

Townson SM, Hanson GR, Upcroft JA, Upcroft P (1994) A purified ferredoxin from Giardia duodenalis. Eur J ^{Biochem 220, 499-446}

Timkovich FR, Dickerson RE Q974) The structure of. Paracoccus denitrificans cyto- chrome cuuo. J Biol Chem 251, 4033-4046

Van Beeumen J, De Ley J, Hall DO, Cammack R, Rao KK (1975) A ferredoxin from Agrobacterium turnefaciens. FEBS Lett 59, ^146-148

Verhagen MFJM, Wolbert RBG, Hagen WR (fggaa) Cytochrome ^csss from Desulfoui-

brio uulgaris (Hildenborough). Electrochemical properties and electron transfer with hydrogenase. Eur J Biochem 221, 82L-829

Verhagen MFJM, Pierik AJ, Wolbert RBG, Mallee LF, Voorhorst WGB, Hagen WR

(1994b) Axial coordination and reduction potentials of the sixteen hemes in ^high-

molecular-mass cytochrome c ^from Desulfouibrio uulgaris ⁽ Hildenborough ) . Eur J Biochem 225, }LL-1L9

Vetter H Jr, Knappe J ⁽¹⁹⁷¹⁾ Flavodoxin and ferredoxin of. Escherichia coli. Hoppe-

Seyler's Z Physiol Chem 352, 433-M6, CA 74:L35270m(fgZf)

慇

Tatsuhiko Yagi

Wagner GC, Kassner RJ, Kamen MD (1974) Redox potentials of certain vitamins K:

Implications for a role in sulfite reduction by obligately anaerobic bacteria. Proc Natl Acad Sci USA 7L, ^253-256

Wallenfels K, Mohle W (1943) tne oxidation-reduction potentials of naphthoquinones.

Chem Ber 768, 924-936

Wang DL, Stankovich MT, Eng LH, Neujahr HY (1991) Redox properties of cytochrome cg from Desulfouibrio desulfuricans NCIMB 8372. Effects of electrode materials and sodium chloride. J Electroanal Chem 318, ^291-307

Watt G D ⁽ 1979) An electrochemical method for measuring redox potentials of low potential proteins by microcoulometry at controlled potentials. Anal Biochem g9, 399- 407

Wermter U, Fischer U ⁽¹⁹⁸³⁾ Molecular properties of high potential iron sulfur protein of. Chromatium warmingii. Z Naturforsch 38c, 968-971

Wissenbach U, Krciger A, Unden G (1990) The specific functions of menaquinone and demethylmenaquinone in anaerobic respiration with fumarate, dimethylsulfoxide, trime- thylamine N-oxide and nitrate by Escherichia coli. Arch Microbiol 154, 60-66

Xavier AV, Moura JJG, LeGall J, DerVartanian DV ^{( fgZg} ) Oxiaation-reduction potentials of the hemes in cytochrome ca from Desulfouibrio gtgas in the ^presence and absence of ferredoxin by EPR spectroscopy. Biochimie 61, ^689-695

Yagi T, Maruyama K (1971) Purification and properties of cytochrome cg of Desul-

fouibrio ^uulgaris Miyazaki. Biochim Biophys Acta 213, 2L4-224

Yagi T ⁽¹⁹⁹⁴⁾ Monoheme cytochromes. Methods Enzymol %13, 104-118 Chapter 8

Yoch DC Q972il The electron transport system in nitrogen fixation by Azotobacter.

IV. Some oxidation-reduction properties of azotoflavin. Biochem Biophys Res Commun 49, 335-342

Yoch DC, Valentine RC (1972b) Four-iron (sulfide) ferredoxin from Bacillus polymyxa.

J Bacteriol 110, I2LL-12L3

Zhu C-X, Song H-Y, Cai J-L, Chou S-M (1982) _Study on the midpoint redox potential

of ferredoxin from Rhodopseudomonas capsulata. Acta Biochim Biophys Sinica 14, 9- 14 (in _Chinese)

Zoephel A, Kennedy MC, Beinert H, Kroneck PMH (1983) Investigations on microbial sulfur respiration. 1. Activation and reduction of elemental sulfur in several strains of eubacteria. Arch Microbiol 150, 72-77

Zubieta JA, Mason R, Postgate JR (1973) A four-iron ferredoxin from Desulfouibrio desulfuricans. Biochem J 133, 851-854

Zweig G, Avron M (1965) On the oxidation-reduction potential of the photoproduced

reductant of isolated chloroplasts. Biochem Biophys Res Commun 19, 397-400