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Fig. 4-14 nuoA lacZ × 3(A) nuoA 3(B) nuoA

× WT

∆arcA

LacZ 3 3

3

Fig. 4-15 Δ Δ MR-1 3Fdh: formate

dehydrogenase 2 Nuo: NADH dehydrogenase 2 c (FccA

CctA)

電極 

Nuo QHQ2

CymA e

-e

-ArcS

ArcA

nuo

発現 

P 4H+

NAD+ NADH

乳酸 

ピルビン酸  アセチルCoA  TCA回路  酢酸 

電極 

dh QH2

Q

CymA e

-e

-ArcS

ArcA

nuo

抑制 

P 乳酸 

ピルビン酸 

アセチルCoA  酢酸  CO2, 2H+

MtrB OmcA/

MtrC MtrA

MtrB OmcA/

MtrC MtrA

Abe, H., Doi, Y., Fukushima, T., Eya, H., 1994. Biosynthesis from gluconate of a random copolyester consisting of 3-hydroxybutyrate and medium-chain-length 3-hydroxyalkanoates by

Pseudomonas sp. 61-3. Int. J. Biol. Macromol. 16, 115–119.

https://doi.org/10.1016/0141-8130(94)90036-1

Bekker, M., Alexeeva, S., Laan, W., Sawers, G., De Mattos, J.T., Hellingwerf, K., 2010. The ArcBA two-component system of Escherichia coli is regulated by the redox state of both the ubiquinone and the menaquinone pool. J. Bacteriol. 192, 746–754. https://doi.org/10.1128/JB.01156-09 Beliaev, A.S., Saffarini, D.A., 1998. Shewanella putrefaciens mtrB encodes an outer membrane

protein required for Fe(III) and Mn(IV) reduction. J. Bacteriol. 180, 6292–6297.

Bongaerts, J., Zoske, S., Weidner, U., Linden, G., 1995. Transcriptional regulation of the proton translocating NADH dehydrogenase (nuoA

N) of Escherichia coli by electron acceptors, electron donors and gene regulators. Mol. Microbiol. 16, 521–534.

https://doi.org/10.1111/j.1365-2958.1995.tb02416.x

Bosch, J., Lee, K.Y., Hong, S.F., Harnisch, F., Schröder, U., Meckenstock, R.U., 2014. Metabolic efficiency of Geobacter sulfurreducens growing on anodes with different redox potentials. Curr.

Microbiol. 68, 763–768. https://doi.org/10.1007/s00284-014-0539-2

Bretschger, O., Obraztsova, A., Sturm, C.A., In, S.C., Gorby, Y.A., Reed, S.B., Culley, D.E., Reardon, C.L., Barua, S., Romine, M.F., Zhou, J., Beliaev, A.S., Bouhenni, R., Saffarini, D., Mansfeld, F., Kim, B.H., Fredrickson, J.K., Nealson, K.H., 2007. Current production and metal oxide

reduction by Shewanella oneidensis MR-1 wild type and mutants. Appl. Environ. Microbiol. 73, 7003–7012. https://doi.org/10.1128/AEM.01087-07

Call, D.F., Wagner, R.C., Logan, B.E., 2009. Hydrogen production by Geobacter species and a mixed consortium in a microbial electrolysis cell. Appl. Environ. Microbiol. 75, 7579–7587.

https://doi.org/10.1128/AEM.01760-09

Claassens, N.J., Sousa, D.Z., Dos Santos, V.A.P.M., De Vos, W.M., Van Der Oost, J., 2016.

Harnessing the power of microbial autotrophy. Nat. Rev. Microbiol. 14, 692–706.

https://doi.org/10.1038/nrmicro.2016.130

Cruz-García, C., Murray, A.E., Rodrigues, J.L.M., Gralnick, J. a, McCue, L.A., Romine, M.F., Löffler, F.E., Tiedje, J.M., 2011. Fnr (EtrA) acts as a fine-tuning regulator of anaerobic metabolism in Shewanella oneidensis MR-1. BMC Microbiol. 11, 64. https://doi.org/10.1186/1471-2180-11-64 Deng, X., Dohmae, N., Nealson, K.H., Hashimoto, K., Okamoto, A., 2018. Multi-heme cytochromes

provide a pathway for survival in energy-limited environments. Sci. Adv. 4, 1–9.

https://doi.org/10.1126/sciadv.aao5682

Deng, X., Okamoto, A., 2018. Electrode potential dependency of single-cell activity identifies the energetics of slow microbial electron uptake process. Front. Microbiol. 9, 1–8.

https://doi.org/10.3389/fmicb.2018.02744

Dibrov, P., Dibrov, E., Pierce, G.N., 2018. Na + -NQR ( Na + -translocating NADH(: ubiquinone oxidoreductase ) as a novel target for antibiotic. FEMS Microbiol. Rev. 41.5, 653–671.

https://doi.org/10.1093/femsre/fux032

Duhl, K. L.; Tefft, N. M.; TerAvest, M.A., 2018. Shewanella oneidensis MR-1 utilizes both sodium- and proton-pumping NADH dehydrogenases during aerobic growth. Appl. Environ. Microbiol.

https://doi.org/10.1128/AEM.00415-18

Efremov, R.G., Baradaran, R., Sazanov, L. a, 2010. The architecture of respiratory complex I. Nature 465, 441–445. https://doi.org/10.1038/nature09066

Endoh, T., Habe, H., Yoshida, T., Nojiri, H., Omori, T., 2003. A CysB-regulated and σ54-dependent regulator, SfnR, is essential for dimethyl sulfone metabolism of Pseudomonas putida strain DS1.

Microbiology 149, 991–1000. https://doi.org/10.1099/mic.0.26031-0

Firer-Sherwood, M., Pulcu, G.S., Elliott, S.J., 2008. Electrochemical interrogations of the Mtr

cytochromes from Shewanella: Opening a potential window. J. Biol. Inorg. Chem. 13, 849–854.

https://doi.org/10.1007/s00775-008-0398-z

Förster, A.H., Beblawy, S., Golitsch, F., Gescher, J., 2017. Biotechnology for Biofuels Electrode

assisted acetoin production in a metabolically engineered Escherichia coli strain. Biotechnol.

Biofuels 1–11. https://doi.org/10.1186/s13068-017-0745-9

Gao, H., Wang, X., Yang, Z.K., Chen, J., Liang, Y., Chen, H., Palzkill, T., Zhou, J., 2010.

Physiological roles of ArcA, Crp, and EtrA and their interactive control on aerobic and anaerobic respiration in Shewanella oneidensis. PLoS One 5, e15295.

https://doi.org/10.1371/journal.pone.0015295

Gao, H., Wang, X., Yang, Z.K., Palzkill, T., Zhou, J., 2008. Probing regulon of ArcA in Shewanella oneidensis MR-1 by integrated genomic analyses. BMC Genomics 9, 42.

https://doi.org/10.1186/1471-2164-9-42

Gorby, Y.A., Yanina, S., Mclean, J.S., Rosso, K.M., Moyles, D., Dohnalkova, A., Beveridge, T.J.,

Chang, I.S., Kim, B.H., Kim, K.S., Culley, D.E., Reed, S.B., Romine, M.F., Saffarini, D.A., Hill,

E.A., Shi, L., Elias, D.A., Kennedy, D.W., Pinchuk, G., Watanabe, K., Ishii, S., Logan, B.,

Nealson, K.H., Fredrickson, J.K., 2006. Electrically conductive bacterial nanowires produced by

Shewanella oneidensis strain MR-1 and other microorganisms. Proc. Natl. Acad. Sci. 103,

11358-11363. https://doi.org/10.1073/pnas.0604517103

Grobbler, C., Virdis, B., Nouwens, A., Harnisch, F., Rabaey, K., Bond, P.L., 2018. Effect of the anode potential on the physiology and proteome of Shewanella oneidensis MR-1. Bioelectrochemistry 119, 172–179. https://doi.org/10.1016/j.bioelechem.2017.10.001

Grobbler, C., Virdis, B., Nouwens, A., Harnisch, F., Rabaey, K., Bond, P.L., 2014. Use of SWATH mass spectrometry for quantitative proteomic investigation of Shewanella oneidensis MR-1 biofilms grown on graphite cloth electrodes. Syst. Appl. Microbiol. 1–5.

https://doi.org/10.1016/j.syapm.2014.11.007

Gunsalus, R.P., Park, S.J., 1994. Aerobic-anaerobic gene regulation in Escherichia coli: control by the ArcAB and Fnr regulons. Res. Microbiol. 145, 437–450.

https://doi.org/10.1016/0923-2508(94)90092-2

Hartshorne, R.S., Reardon, C.L., Ross, D., Nuester, J., Clarke, T.A., Gates, A.J., Mills, P.C., Fredrickson, J.K., Zachara, J.M., Shi, L., Beliaev, A.S., Marshall, M.J., Tien, M., Brantley, S., Butt, J.N., Richardson, D.J., 2009. Characterization of an electron conduit between bacteria and the extracellular environment. Proc. Natl. Acad. Sci. 106, 22169–22174.

https://doi.org/10.1073/pnas.0900086106

Heidelberg, J.F., Paulsen, I.T., Nelson, K.E., Gaidos, E.J., Nelson, W.C., Read, T.D., Eisen, J.A., Seshadri, R., Ward, N., Methe, B., Clayton, R.A., Meyer, T., Tsapin, A., Scott, J., Beanan, M., Brinkac, L., Daugherty, S., DeBoy, R.T., Dodson, R.J., Durkin, A.S., Haft, D.H., Kolonay, J.F., Madupu, R., Peterson, J.D., Umayam, L.A., White, O., Wolf, A.M., Vamathevan, J., Weidman, J., Impraim, M., Lee, K., Berry, K., Lee, C., Mueller, J., Khouri, H., Gill, J., Utterback, T.R., McDonald, L.A., Feldblyum, T. V., Smith, H.O., Venter, J.C., Nealson, K.H., Fraser, C.M., 2002.

Genome sequence of the dissimilatory metal ion-reducing bacterium Shewanella oneidensis. Nat.

Biotechnol. 20, 1118–1123. https://doi.org/10.1038/nbt749

Hirose, A., Kasai, T., Koga, R., Suzuki, Y., Kouzuma, A., Watanabe, K., 2019a. Understanding and engineering electrochemically active bacteria for sustainable biotechnology. Bioresour.

Bioprocess. 1–15. https://doi.org/10.1186/s40643-019-0245-9

Hirose, A., Kouzuma, A., Watanabe, K., 2019b. Towards development of electrogenetics using electrochemically active bacteria. Biotechnol. Adv.

https://doi.org/10.1016/j.biotechadv.2019.02.007

Hunt, K.A., Flynn, J.M., Naranjo, B., Shikhare, I.D., Gralnick, J.A., 2010. Substrate-level

phosphorylation is the primary source of energy conservation during anaerobic respiration of

Shewanella oneidensis strain MR-1. J. Bacteriol. 192, 3345–3351.

https://doi.org/10.1128/JB.00090-10

Ishii, M., Takishita, S., Iwasaki, T., Peerapornpisal, Y., Yoshino, J., Kodama, T., Igarashi, Y., 2000.

Purification and Characterization of Membrane-bound Hydrogenase from Hydrogenobacter thermophilus Strain TK-6, an Obligately Autotrophic, Thermophilic, Hydrogen-oxidizing Bacterium. Biosci. Biotechnol. Biochem. 64, 492–502. https://doi.org/10.1271/bbb.64.492 Ishii, S., Kosaka, T., Hori, K., Hotta, Y., Watanabe, K., 2005. Coaggregation facilitates interspecies

hydrogen transfer between Pelotomaculum thermopropionicum and Methanothermobacter thermautotrophicus. Appl. Environ. Microbiol. 71, 7838–7845.

https://doi.org/10.1128/AEM.71.12.7838-7845.2005

Ishii, T., Kawaichi, S., Nakagawa, H., Hashimoto, K., Nakamura, R., 2015. From

chemolithoautotrophs to electrolithoautotrophs: CO2 fixation by Fe(II)-oxidizing bacteria coupled with direct uptake of electrons from solid electron sources. Front. Microbiol. 6, 1–9.

https://doi.org/10.3389/fmicb.2015.00994

Jones, S.W., Fast, A.G., Carlson, E.D., Wiedel, C.A., Au, J., Antoniewicz, M.R., Papoutsakis, E.T., Tracy, B.P., 2016. CO2 fixation by anaerobic non-photosynthetic mixotrophy for improved carbon conversion. Nat. Commun. 7, 12800. https://doi.org/10.1038/ncomms12800

Kane, A.L., Brutinel, E.D., Joo, H., Maysonet, R., VanDrisse, C.M., Kotloski, N.J., Gralnick, J.A., 2016. Formate metabolism in Shewanella oneidensis generates proton motive force and prevents growth without an electron acceptor. J. Bacteriol. 198, 1337–1346.

https://doi.org/10.1128/JB.00927-15

Karthikeyan, R., Singh, R., Bose, A., 2019. Microbial electron uptake in microbial electrosynthesis(: a mini

review. J. Ind. Microbiol. Biotechnol. https://doi.org/10.1007/s10295-019-02166-6 Kasai, T., Kouzuma, A., Nojiri, H., Watanabe, K., 2015. Transcriptional mechanisms for differential

expression of outer membrane cytochrome genes omcA and mtrC in Shewanella oneidensis MR-1. BMC Microbiol. 15, 68. https://doi.org/10.1186/s12866-015-0406-8

Kasai, T., Kouzuma, A., Watanabe, K., 2017. CRP regulates D-lactate oxidation in Shewanella oneidensis MR-1. Front. Microbiol. 8, 1–11. https://doi.org/10.3389/fmicb.2017.00869

Kasai, T., Suzuki, Y., Kouzuma, A., Watanabe, K., 2019. Roles of D -Lactate Dehydrogenases in the Anaerobic Growth of Shewanella oneidensis MR-1 on Sugars. Appl. Environ. Microbiol. 85, 1–

11. https://doi.org/10.1128/AEM.02668-18

Kimura, Z.I., Okabe, S., 2013. Acetate oxidation by syntrophic association between Geobacter sulfurreducens and a hydrogen-utilizing exoelectrogen. ISME J. 7, 1472–1482.

https://doi.org/10.1038/ismej.2013.40

Kitayama, M., Koga, R., Kasai, T., Kouzuma, A., Watanabe, K., 2017. Structures, compositions, and activities of live Shewanella biofilms formed on graphite electrodes in electrochemical flow cells.

Appl. Environ. Microbiol. 83, 1–11. https://doi.org/10.1128/AEM.00903-17

Kouzuma, A., Hashimoto, K., Watanabe, K., 2012. Roles of siderophore in manganese-oxide reduction by Shewanella oneidensis MR-1. FEMS Microbiol. Lett. 326, 91–98.

https://doi.org/10.1111/j.1574-6968.2011.02444.x

Kracke, F., Vassilev, I., Kr??mer, J.O., 2015. Microbial electron transport and energy conservation - The foundation for optimizing bioelectrochemical systems. Front. Microbiol. 6, 1–18.

https://doi.org/10.3389/fmicb.2015.00575

Lassak, J., Bubendorfer, S., Thormann, K.M., 2013. Domain analysis of ArcS, the hybrid sensor kinase of the Shewanella oneidensis MR-1 Arc two-component system, reveals functional differentiation of its two receiver domains. J. Bacteriol. 195, 482–92.

https://doi.org/10.1128/JB.01715-12

Lassak, J., Henche, A.-L., Binnenkade, L., Thormann, K.M., 2010. ArcS, the cognate sensor kinase in an atypical Arc system of Shewanella oneidensis MR-1. Appl. Environ. Microbiol. 76, 3263–74.

https://doi.org/10.1128/AEM.00512-10

Le Laz, S., Kpebe, A., Lorquin, J., Brugna, M., Rousset, M., 2014. H2-dependent azoreduction by Shewanella oneidensis MR-1: Involvement of secreted flavins and both [Ni-Fe] and [Fe-Fe]

hydrogenases. Appl. Microbiol. Biotechnol. 98, 2699–2707.

https://doi.org/10.1007/s00253-013-5208-z

Levar, C.E., Hoffman, C.L., Dunshee, A.J., Toner, B.M., Bond, D.R., 2017. Redox potential as a master variable controlling pathways of metal reduction by Geobacter sulfurreducens. ISME J.

11, 741–752. https://doi.org/10.1038/ismej.2016.146

Li, D.B., Li, J., Liu, D.F., Ma, X., Cheng, L., Li, W.W., Qian, C., Mu, Y., Yu, H.Q., 2019. Potential regulates metabolism and extracellular respiration of electroactive Geobacter biofilm. Biotechnol.

Bioeng. 116, 961–971. https://doi.org/10.1002/bit.26928

Lian, Y., Yang, Y., Guo, J., Wang, Y., Li, X., Fang, Y., Gan, L., Xu, M., 2016. Electron acceptor redox potential globally regulates transcriptomic profiling in Shewanella decolorationis S12. Sci.

Rep. 6, 1–9. https://doi.org/10.1038/srep31143

Light, S.H., Su, L., Rivera-lugo, R., Cornejo, J.A., Louie, A., Iavarone, A.T., 2018. A flavin-based extracellular electron transfer mechanism in diverse Gram-positive bacteria. Nature.

https://doi.org/10.1038/s41586-018-0498-z

Lin, E.C.C., 1996. Transcriptional control mediated by the ArcA two-component response regulator

protein of Escherichia coli(: characterization of DNA binding at target promoters. J. Bacteriol.

178, 6238–6249. https://doi.org/10.1128/jb.178.21.6238-6249.1996

Liu, C., Gorby, Y.A., Zachara, J.M., Fredrickson, J.K., Brown, C.F., 2002. Reduction kinetics of Fe(III), Co(III), U(VI), Cr(VI), and Tc(VII) in cultures of dissimilatory metal-reducing bacteria.

Biotechnol. Bioeng. 80, 637–649. https://doi.org/10.1002/bit.10430

Logan, B.E., 2009. Exoelectrogenic bacteria that power microbial fuel cells. Nat. Rev. Microbiol. 7, 375–381. https://doi.org/10.1038/nrmicro2113

Madsen, C.S., TerAvest, M.A., 2019. NADH dehydrogenases contribute to extracellular electron transfer by Shewanella oneidensis MR-1 in bioelectrochemical systems. bioRxiv 1–15.

https://doi.org/http://dx.doi.org/10.1101/657668

Marshall, M.J., Plymale, A.E., Kennedy, D.W., Shi, L., Wang, Z., Reed, S.B., Dohnalkova, A.C., Simonson, C.J., Liu, C., Saffarini, D.A., Romine, M.F., Zachara, J.M., Beliaev, A.S., Fredrickson, J.K., 2008. Hydrogenase- and outer membrane c-type cytochrome-facilitated reduction of technetium(VII) by Shewanella oneidensis MR-1. Environ. Microbiol. 10, 125–136.

https://doi.org/10.1111/j.1462-2920.2007.01438.x

McMillan, D.G.G., Marritt, S.J., Butt, J.N., Jeuken, L.J.C., 2012. Menaquinone-7 is specific cofactor in tetraheme quinol dehydrogenase CymA. J. Biol. Chem. 287, 14215–14225.

https://doi.org/10.1074/jbc.M112.348813

Melo, A.M.P., Bandeiras, T.M., Teixeira, M., 2004. New Insights into Type II NAD ( P ) H(: Quinone Oxidoreductases. Microbiol. Mol. Biol. Rev. 68, 603–616.

https://doi.org/10.1128/MMBR.68.4.603

Meshulam-simon, G., Behrens, S., Choo, A.D., Spormann, A.M., 2007. Hydrogen Metabolism in Shewanella oneidensis MR-1. Appl. Environ. Microbiol. 73, 1153–1165.

https://doi.org/10.1128/AEM.01588-06

Moscoviz, R., Toledo-Alarcón, J., Trably, E., Bernet, N., 2016. Electro-Fermentation: How To Drive Fermentation Using Electrochemical Systems. Trends Biotechnol. 34, 856–865.

https://doi.org/10.1016/j.tibtech.2016.04.009

Myers, C.R., Nealson, K.H., 1988. Bacterial manganese reduction and growth with manganese oxide as the sole electron acceptor. Science. 240, 1319–1321.

https://doi.org/10.1126/science.240.4857.1319

Myers, J.M., Myers, C.R., 2000. Role of the tetraheme cytochrome CymA in anaerobic electron transport in cells of Shewanella putrefaciens MR-1 with normal levels of menaquinone. J.

Bacteriol. 182, 67–75. https://doi.org/10.1128/JB.182.1.67-75.2000

Myers, K.S., Yan, H., Ong, I.M., Chung, D., Liang, K., Tran, F., Keleş, S., Landick, R., Kiley, P.J., 2013. Genome-scale Analysis of Escherichia coli FNR Reveals Complex Features of

Transcription Factor Binding. PLoS Genet. 9, 11–13.

https://doi.org/10.1371/journal.pgen.1003565

Nakagawa, G., Kouzuma, A., Hirose, A., Kasai, T., Yoshida, G., Watanabe, K., 2015. Metabolic Characteristics of a Glucose-Utilizing Shewanella oneidensis Strain Grown under

Electrode-Respiring Conditions. PLoS One 10, e0138813.

https://doi.org/10.1371/journal.pone.0138813

Nakamura, R., Takashima, T., Kato, S., Takai, K., Yamamoto, M., Hashimoto, K., 2010. Electrical current generation across a black smoker chimney. Angew. Chemie - Int. Ed. 49, 7692–7694.

https://doi.org/10.1002/anie.201003311

Nealson, K.H., Saffarini, D., 1994. Iron and manganese in anaerobic respiration: environmental significance, physiology, and regulation. Annu. Rev. Microbiol. 48, 311–343.

https://doi.org/10.1146/annurev.micro.48.1.311

Pankratova, G., Szypulska, E., Pankratov, D., Leech, D., Gorton, L., 2019. Electron Transfer between the Gram-Positive Enterococcus faecalis Bacterium and Electrode Surface through Osmium Redox Polymers. ChemElectroChem 6, 110–113. https://doi.org/10.1002/celc.201800683 Park, D.M., Akhtar, M.S., Ansari, A.Z., Landick, R., Kiley, P.J., 2013. The bacterial response

regulator ArcA uses a diverse binding site architecture to regulate carbon oxidation globally.

PLoS Genet. 9, e1003839. https://doi.org/10.1371/journal.pgen.1003839

Pinchuk, G.E., Geydebrekht, O. V, Hill, E. a, Reed, J.L., Konopka, A.E., Beliaev, A.S., Fredrickson, J.K., 2011. Pyruvate and lactate metabolism by Shewanella oneidensis MR-1 under fermentation, oxygen limitation, and fumarate respiration conditions. Appl. Environ. Microbiol. 77, 8234–40.

https://doi.org/10.1128/AEM.05382-11

Pinchuk, G.E., Hill, E. a., Geydebrekht, O. V., de Ingeniis, J., Zhang, X., Osterman, A., Scott, J.H., Reed, S.B., Romine, M.F., Konopka, A.E., Beliaev, A.S., Fredrickson, J.K., Reed, J.L., 2010.

Constraint-based model of Shewanella oneidensis MR-1 metabolism: A tool for data analysis and hypothesis generation. PLoS Comput. Biol. 6, 1–8.

https://doi.org/10.1371/journal.pcbi.1000822

Pirbadian, S., Barchinger, S.E., Man, K., Suk, H., Jangir, Y., Bouhenni, R.A., 2014. Shewanella oneidensis MR-1 nanowires are outer membrane and periplasmic extensions of the extracellular electron transport components. Proc. Natl. Acad. Sci. 111, 12883-12888.

https://doi.org/10.1073/pnas.1410551111

Pradella, S., Hippe, H., Stackebrandt, E., 1998. Macrorestriction analysis of Desulfurella acetivorans and Desulfurella multipotens. FEMS Microbiol. Lett. 159, 137–144.

https://doi.org/10.1016/S0378-1097(97)00561-2

Rabaey, K., Rozendal, R.A., 2010. Microbial electrosynthesis - Revisiting the electrical route for microbial production. Nat. Rev. Microbiol. 8, 706–716. https://doi.org/10.1038/nrmicro2422 Reysenbach, A.L., Shock, E., 2002. Merging genomes with geochemistry in hydrothermal ecosystems.

Science. 296, 1077–1082. https://doi.org/10.1126/science.1072483

Rodionov, D.A., Yang, C., Li, X., Rodionova, I.A., Wang, Y., Obraztsova, A.Y., Zagnitko, O.P., Overbeek, R., Romine, M.F., Reed, S., Fredrickson, J.K., Nealson, K.H., Osterman, A.L., 2010.

Genomic encyclopedia of sugar utilization pathways in the Shewanella genus. BMC Genomics 11. https://doi.org/10.1186/1471-2164-11-494

Ross, D.E., Flynn, J.M., Baron, D.B., Gralnick, J.A., Bond, D.R., 2011. Towards Electrosynthesis in Shewanella(: Energetics of Reversing the Mtr Pathway for Reductive Metabolism. PLoS One 6.

https://doi.org/10.1371/journal.pone.0016649

Rowe, A.R., Rajeev, P., Jain, A., Pirbadian, S., Okamoto, A., Gralnick, J.A., El-Naggar, M.Y., Nealson, K.H., 2018. Tracking electron uptake from a cathode into Shewanella cells:

Implications for energy acquisition from solid-substrate electron donors. MBio 9, 1–19.

https://doi.org/10.1128/mBio.02203-17

Saffarini, D. a, Schultz, R., Beliaev, A., 2003. Involvement of Cyclic AMP ( cAMP ) and cAMP Receptor Protein in Anaerobic Respiration of Shewanella oneidensis. J. Bacteriol. 185, 3668–

3671. https://doi.org/10.1128/JB.185.12.3668

Sharma, P., Stagge, S., Bekker, M., Bettenbrock, K., Hellingwerf, K.J., 2013. Kinase Activity of ArcB from Escherichia coli Is Subject to Regulation by Both Ubiquinone and Demethylmenaquinone.

PLoS One 8. https://doi.org/10.1371/journal.pone.0075412

Shi, L., Chen, B., Wang, Z., Elias, D.A., Mayer, M.U., Gorby, Y.A., Ni, S., Lower, B.H., Kennedy, D.W., Wunschel, D.S., Mottaz, H.M., Marshall, M.J., Hill, E.A., Beliaev, A.S., Zachara, J.M., Fredrickson, J.K., Squier, T.C., 2006. Isolation of a high-affinity functional protein complex between OmcA and MtrC: Two outer membrane decaheme c-type cytochromes of Shewanella oneidensis MR-1. J. Bacteriol. 188, 4705–4714. https://doi.org/10.1128/JB.01966-05

Simon, J., van Spanning, R.J.M., Richardson, D.J., 2008. The organisation of proton motive and non-proton motive redox loops in prokaryotic respiratory systems. Biochim. Biophys. Acta - Bioenerg. 1777, 1480–1490. https://doi.org/10.1016/j.bbabio.2008.09.008

Spero, M. a, Aylward, F.O., Currie, C.R., Donohue, T.J., 2015. Phylogenomic Analysis and Predicted

Physiological Role of the Proton-Translocating NADH:Quinone Oxidoreductase (Complex I) Across Bacteria. MBio 6, e00389-15-. https://doi.org/10.1128/mBio.00389-15

Sturm-richter, K., Golitsch, F., Sturm, G., Kipf, E., Dittrich, A., Beblawy, S., Kerzenmacher, S., Gescher, J., 2015. Unbalanced fermentation of glycerol in Escherichia coli via heterologous production of an electron transport chain and electrode interaction in microbial electrochemical cells. Bioresour. Technol. 186, 89–96. https://doi.org/10.1016/j.biortech.2015.02.116

Sturm, G., Richter, K., Doetsch, A., Heide, H., Louro, R.O., Gescher, J., 2015. A dynamic periplasmic electron transfer network enables respiratory flexibility beyond a thermodynamic regulatory regime. ISME J. 9, 1802–1811. https://doi.org/10.1038/ismej.2014.264

Tang, Y.J., Hwang, J.S., Wemmer, D.E., Keasling, J.D., 2007. Shewanella oneidensis MR-1 fluxome under various oxygen conditions. Appl. Environ. Microbiol. 73, 718–29.

https://doi.org/10.1128/AEM.01532-06

Tefft, N.M., Teravest, M.A., 2019. Reversing an Extracellular Electron Transfer Pathway for Electrode-Driven Acetoin Reduction. ACS Synth. Biol.

https://doi.org/10.1021/acssynbio.8b00498

Teran-Melo, J.L., Peña-Sandoval, G.R., Silva-Jimenez, H., Rodriguez, C., Alvarez, A.F., Georgellis, D., 2018. Routes of phosphoryl-group transfer during signal transmission and signal decay in the dimeric sensor histidine kinase ArcB. J. Biol. Chem. 293, jbc.RA118.003910.

https://doi.org/10.1074/jbc.RA118.003910

Tran, Q.H., Bongaerts, J., Vlad, D., Unden, G., 1997. Requirement for the proton-pumping NADH dehydrogenase I of Escherichia coli in respiration of NADH to fumarate and its bioenergetic implications. Eur. J. Biochem. 244, 155–160.

https://doi.org/10.1111/j.1432-1033.1997.00155.x

Venkateswaran, K., Moser, D.P., Dollhopf, M.E., Lies, D.P., Saffarini, D. a, MacGregor, B.J.,

Ringelberg, D.B., White, D.C., Nishijima, M., Sano, H., Burghardt, J., Stackebrandt, E., Nealson, K.H., 1999. Polyphasic taxonomy of the genus Shewanella and description of Shewanella

oneidensis sp. nov. Int. J. Syst. Bacteriol. 49, 705–724.

https://doi.org/10.1099/00207713-49-2-705

Wu, Z., Wang, J., Liu, J., Wang, Y., Bi, C., Zhang, X., 2019a. Engineering an electroactive

Escherichia coli for the microbial electrosynthesis of succinate from glucose and CO2. Microb.

Cell Fact. 18, 1–14. https://doi.org/10.1186/s12934-019-1067-3

Wu, Z., Wang, J., Zhang, X., Bi, C., 2019b. Engineering an electroactive Escherichia coli for the

microbial electrosynthesis of succinate by increasing the intracellular FAD pool. Biochem. Eng. J.

146, 132–142. https://doi.org/10.1016/j.bej.2019.03.015

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(1) Nakagawa, G., Kouzuma, A., Hirose, A., Kasai, T., Yoshida, G., & Watanabe, K. (2015).

Metabolic characteristics of a glucose-utilizing Shewanella oneidensis strain grown under electrode-respiring conditions. PloS one, 10(9), e0138813.

(2) Hirose, A., Kasai, T., Aoki, M., Umemura, T., Watanabe, K., & Kouzuma, A. (2018).

Electrochemically active bacteria sense electrode potentials for regulating catabolic pathways. Nature communications, 9(1), 1-10.

2

(1) Kouzuma A, Kasai T, Hirose A, & Watanabe K (2015). Catabolic and regulatory systems in Shewanella oneidensis MR-1 involved in electricity generation in microbial fuel cells.

Frontiers in microbiology, 6, 609.

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47:74-79.

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58:33-38

(4) 2 2 . 12 .

. CMC .

(5) 2 2 2 . Shewanella

. .

(6) Hirose, A., Kouzuma, A., & Watanabe, K. (2019). Towards development of

electrogenetics using electrochemically active bacteria. Biotechnology advances, 37(6), 107351.

(7) Hirose, A., Kasai, T., Koga, R., Suzuki, Y., Kouzuma, A., & Watanabe, K. (2019).

Understanding and engineering electrochemically active bacteria for sustainable biotechnology. Bioresources and Bioprocessing, 6(1), 10.

(8) Inohana Y, Matsumoto A, Nagoya M, Hirose A, Kouzuma A, Watanabe K. Rice paddy-field microbial fuel cells: fundamental and recent progress. Bio-electrochemical systems: A sustainable platform for fuels and chemicals. Springer/nature. In press.

(1)

○Hirose A., Kouzuma A., Watanabe K. Molecular mechanisms for sensing and

responding to electrode potentials in Shewanella oneidensis MR-1. Bio micro world 2015, Barcelona, Spain, October, 2015.

(2)

○Hirose A., Kouzuma A., Aoki M., Umemura T., Watanabe K. Electrode

potential-dependent energy conservation in Shewanella oneidensis MR-1. ISME 16,

Montreal, Canada, August, 2016

(3)

Hirose A., Kasai T., Kouzuma A. and ○Watanabe K. Shewanella senses electrode potential for catabolic regulation. The 3rd European Meeting of the International Society for Microbial Electrochemistry and Technology, Rome, Italy, September, 2016.

(4)

Hirose A., Kasai T., Kouzuma A. and ○Watanabe K. Shewanella senses electrode potential for catabolic regulation. The 3rd Asian-Pacific Meeting of the International Society for Microbial Electrochemistry and Technology, Busan, South Korea, August,

2016. .

(5)

○Kouzuma A., Hirose A., Mogi H., Kasai T., and Watanabe K. A novel mode of

regulation for electrochemical activities of Shewanella oneidensis MR-1. International Society for Microbial Electrochemistry and Technology, Okinawa, Japan, October, 2019.

(1)

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○Hirose A., Kouzuma A. and Watanabe K. Molecular mechanisms for sensing and

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○Hirose A., Kouzuma A. and Watanabe K.

Shewanella oneidensis MR-1, an

electrochemically active bacteria; its fundamentals and applications. The 16th

International Symposium on Advanced Technology, Tokyo, Japan, November 2017.

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Appendix

Appendix 1

Strain or plasmid Relevant characteristic Source of reference Escherichia coli

DH5α F-, φ 80dlacZ∆M15, ∆(lacZYA-argF)U169, deoR, recA1, endA1, hsdR17(rK-, mK+), phoA, supE44, λ-, thi-1,

gyrA96, relA1

Takara

JM109 recA1. endAl, gyrA96, thi. hsdR17, supE44, relA1, λ-,

∆(lac-proAB), [F’, traD36, proAB, lacIq Z∆M15]

Takara JM109λpir JM109 lysogenized with λpir Penfold and

Pemberton, 1992 WM6026 lacIq, rrnB3, DElacZ4787, hsdR514, DE(araBAD)567,

E(rhaBAD)568, rph-1,

att-lambda::pAE12-del(oriR6K-cat::frt5), DE(endA)::frt, uidA(delMluI)::pir(wt), attHK::pJK1006-del1/2

(deloriR6K-cat::frt5, deltrfA::frt)

William Metcalf, University of Illinois

BL21 DE3 F ompT hsdR17 (rB mB+) gal dcm(DE3) F, ompT, hsdSB (rB mB), gal(λcI 857, ind1, sam7, nin5,

lacUV5-T7gene1), dcm(DE3)

Novagen

S. oneidensis strain

MR-1 Wild type ATCC

ΔPFL SO_2912 pflB disruption This study ΔPDH SO_0424 aceE disruption This study ΔNDH SO_1017 nuoF , SO_3517 ndh , SO_0907 nqrF-1 ,

SO_1108 nqrF-2 disruption

This study ΔarcS SO_0577 arcS disruption This study ΔarcA SO_3988 arcA disruption This study ΔhyaB SO_2098 hyaB disruption This study ΔhydA SO_3920 hydA disruption This study ΔhydAΔhyaB SO_2098 hyaB , SO_3920 hydA disruption This study Δatp SO_4746 atpC to SO_4754 atpI disruption This study ΔubiA SO_0468 (ubiA) disruption This study ΔmenA SO_1910 (menA) disruption This study

ΔnuoF SO_1017 nuoF This study

Δndh SO_3517 ndh This study

ΔnqrF-1 SO_0907 nqrF-1 This study

ΔnqrF-2 SO_1108 nqrF-2 This study

ΔnuoFΔndh SO_1017 nuoF , SO_3517 ndh disruption This study ΔnuoFΔNDHΔubiA SO_1017 (nuoF), SO_3517 (ndh), SO_0468 (ubiA)

disruption

This study ΔnuoFΔNDHΔmenA SO_1017 (nuoF), SO_3517 (ndh), SO_1910 menA

disruption

This study NUO SO_3517 ndh , SO_0907 nqrF-1 , SO_1108 nqrF-2

disruption

This study NDH SO_1017 nuoF , SO_0907 nqrF-1 , SO_1108

nqrF-2 disruption

This study NQR1 SO_1017 nuoF , SO_3517 ndh , SO_1108 nqrF-2

disruption

This study NQR2 SO_1017 nuoF , SO_3517 ndh , SO_0907 nqrF-1

disruption

This study ΔcymA SO_4591 (cymA) disruption Bretschger et al.

2007

Appendix 1

Strain or plasmid Relevant characteristic Source of reference (omcA(mtrC SO_1779 (omcA), SO_1778 (mtrC) disruptionn Bretschger et al.

2007 ΔetrA SO_2356 (etrA) disruption This study Plasmid

pET-28 a Expression vector, T7 promoter Novagen

pET-arcA pET-28(a) containing N terminal His-tag-arcA This study pSMV-10 9.1 kb mobilizable suicide vector; oriR6K, mobRP4,

sacB, Kmr, Gmr

Chad Saltikov, California Inst. of

Tech.

pSMV-pfl 1.6 kb fusion PCR fragment containing ∆pfl cloned into the SpeI site of pSMV-10

This study pSMV-aceE 1.6 kb fusion PCR fragment containing ∆aceE cloned

into the SpeI site of pSMV-10

This study pSMV-nuoF 1.6 kb fusion PCR fragment containing ∆nuoF cloned

into the SpeI site of pSMV-10

This study pSMV-ndh 1.6 kb fusion PCR fragment containing ∆ndh cloned into

the SpeI site of pSMV-10

This study pSMV-nqrF-1 1.6 kb fusion PCR fragment containing ∆nqrF-1 cloned

into the SpeI site of pSMV-10

This study pSMV-nqrF-2 1.6 kb fusion PCR fragment containing ∆nqrF-2 cloned

into the SpeI site of pSMV-10

This study pSMV-arcS 1.6 kb fusion PCR fragment containing ∆arcS cloned

into the SpeI site of pSMV-10

This study pSMV-arcA 1.6 kb fusion PCR fragment containing ∆arcA cloned

into the SpeI site of pSMV-10

This study pSMV-atp 1.6 kb fusion PCR fragment containing ∆atp cloned into

the SpeI site of pSMV-10

This study pSMV-hyaB 1.6 kb fusion PCR fragment containing ∆hyaB cloned

into the SpeI site of pSMV-10

This study pSMV-hydA 1.6 kb fusion PCR fragment containing ∆hydA cloned

into the SpeI site of pSMV-10

This study pSMV-ubiA 1.6 kb fusion PCR fragment containing ∆ubiA cloned

into the SpeI site of pSMV-10

This study pSMV-menA 1.6 kb fusion PCR fragment containing ∆menA cloned

into the SpeI site of pSMV-10

This study pSMV-etrA 1.6 kb fusion PCR fragment containing ∆etrA cloned into

the SpeI site of pSMV-10

This study pMElacZ pME4510 derivative, lacZ Gmr Endoh et al. 2003 pME-PnuoA pMElacZ containing nuoA upstream region This study pME-PnuoA_TSS-7 pMElacZ containing region from -7 to +163 relative to

TSSnuoA

This study pME-PnuoA_TSS-63 pMElacZ containing region from -63 to +163 relative to

TSSnuoA

This study pME-PnuoA_TSS-112 pMElacZ containing region from -112 to +163 relative

to TSSnuoA

This study pME-PnuoA_TSS-273 pMElacZ containing region from -273 to +163 relative

to TSSnuoA

This study pME-PnuoA_TSS-361 pMElacZ containing region from -361 to +163 relative

to TSSnuoA

This study pME-PnuoA_TSS-407 pMElacZ containing region from -407 to +163relative

to TSSnuoA

This study pME-Pndh pMElacZ containing ndh upstream region This study pME-Pnqr1 pMElacZ containing nqr1 upstream region This study pME-Pnqr2 pMElacZ containing nqr2 upstream region This study

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