143. Edwards MJ, White GF, Lockwood CW, Lawes MC, Martel A, Harris G, Scott DJ,
Richardson DJ, Butt JN, Clarke TA (2018) Structural modeling of an outer membrane
electron conduit from a metal-reducing bacterium suggests electron transfer via periplasmic
redox partners. J Biol Chem 293:8103–8112. https://doi.org/10.1074/jbc.RA118.001850
144. Ross DE, Ruebush SS, Brantley SL, Hartshorne RS, Clarke TA, Richardson DJ, Tien M
(2007) Characterization of protein-protein interactions involved in iron reduction by
Shewanella oneidensis MR-1. Appl Environ Microbiol 73:5797–5808. https://doi.org/10.
1128/AEM.00146-07
145. Pitts KE, Dobbin PS, Reyes-Ramirez F, Thomson AJ, Richardson DJ, Seward HE (2003)
Characterization of the Shewanella oneidensis MR-1 decaheme cytochrome MtrA:
expression in Escherichia coli confers the ability to reduce soluble FE(III) chelates. J Biol
Chem 278:27758–27765. https://doi.org/10.1074/jbc.M302582200
146. Clarke TA, Cole JA, Richardson DJ, Hemmings AM (2007) The crystal structure of the
pentahaem c-type cytochrome NrfB and characterization of its solution-state interaction with
the pentahaem nitrite reductase NrfA. Biochem J 406:19–30. https://doi.org/10.1042/
BJ20070321
147. Matias VRF, Al-Amoudi A, Dubochet J, Beveridge TJ (2003) Cryo-transmission electron
microscopy of frozen-hydrated sections of Escherichia coli and Pseudomonas aeruginosa.
J Bacteriol 185:6112–6118. https://doi.org/10.1128/JB.185.20.6112-6118.2003
148. Myers CR, Myers JM (2003) Cell surface exposure of the outer membrane cytochromes of
Shewanella oneidensis MR-1. Lett Appl Microbiol 37:254–258. https://doi.org/10.1046/j.
1472-765X.2003.01389.x
149. Myers JM, Myers CR (2001) Role for outer membrane cytochromes OmcA and OmcB of
Shewanella putrefaciens MR-1 in reduction of manganese dioxide. Appl Environ Microbiol
67:260–269. https://doi.org/10.1128/AEM.67.1.260
150. Zhang H, Tang X, Munske GR, Tolic N, Anderson GA, Bruce JE (2009) Identification of
protein-protein interactions and topologies in living cells with chemical cross-linking and
mass spectrometry. Mol Cell Proteomics 8:409–420. https://doi.org/10.1074/mcp.M800232MCP200
151. Shi L, Chen B, Wang Z, Elias DA, Mayer MU, Gorby YA, Ni S, Lower BH, Kennedy DW,
Wunschel DS, Mottaz HM, Marshall MJ, Hill EA, Beliaev AS, Zachara JM, Fredrickson JK,
Squier TC (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
152. Borloo J, Vergauwen B, De Smet L, Brigé A, Motte B, Devreese B, Van Beeumen J, De SL,
Brige A, Motte B, Devreese B, Van BJJ (2007) A kinetic approach to the dependence of
dissimilatory metal reduction by Shewanella oneidensis MR-1 on the outer membrane
cytochromes c OmcA and OmcB. FEBS J 274:3728–3738. https://doi.org/10.1111/j.17424658.2007.05907.x
153. Xiong Y, Shi L, Chen B, Mayer MU, Lower BH, Londer YY, Bose S, Hochella MF,
Fredrickson JK, Squier TC (2006) High-affinity binding and direct electron transfer to solid
metals by the Shewanella oneidensis MR-1 outer membrane c-type cytochrome OmcA.
J Am Chem Soc 128:13978–13979. https://doi.org/10.1021/ja063526d
154. Meitl LA, Eggleston CM, Colberg PJS, Khare N, Reardon CL, Shi L (2009) Electrochemical
interaction of Shewanella oneidensis MR-1 and its outer membrane cytochromes OmcA and
MtrC with hematite electrodes. Geochim Cosmochim Acta 73:5292–5307. https://doi.org/
10.1016/j.gca.2009.06.021
155. Eggleston CM, Vo J, Droubay TC, Colberg PJS (2008) Binding and direct electrochemistry
of OmcA, an outer-membrane cytochrome from an iron reducing bacterium, with oxide
electrodes: a candidate biofuel cell system. Inorganica Chim Acta 361:769–777. https://doi.
org/10.1016/j.ica.2007.07.015
156. Lower BH, Lins RD, Oestreicher Z, Straatsma TP, Hochella MF, Shi L, Lower SK (2008) In
vitro evolution of a peptide with a hematite binding motif that may constitute a natural
Bacterial Power: An Alternative Energy Source
243
Richardson DJ, Butt JN, Clarke TA (2018) Structural modeling of an outer membrane
electron conduit from a metal-reducing bacterium suggests electron transfer via periplasmic
redox partners. J Biol Chem 293:8103–8112. https://doi.org/10.1074/jbc.RA118.001850
144. Ross DE, Ruebush SS, Brantley SL, Hartshorne RS, Clarke TA, Richardson DJ, Tien M
(2007) Characterization of protein-protein interactions involved in iron reduction by
Shewanella oneidensis MR-1. Appl Environ Microbiol 73:5797–5808. https://doi.org/10.
1128/AEM.00146-07
145. Pitts KE, Dobbin PS, Reyes-Ramirez F, Thomson AJ, Richardson DJ, Seward HE (2003)
Characterization of the Shewanella oneidensis MR-1 decaheme cytochrome MtrA:
expression in Escherichia coli confers the ability to reduce soluble FE(III) chelates. J Biol
Chem 278:27758–27765. https://doi.org/10.1074/jbc.M302582200
146. Clarke TA, Cole JA, Richardson DJ, Hemmings AM (2007) The crystal structure of the
pentahaem c-type cytochrome NrfB and characterization of its solution-state interaction with
the pentahaem nitrite reductase NrfA. Biochem J 406:19–30. https://doi.org/10.1042/
BJ20070321
147. Matias VRF, Al-Amoudi A, Dubochet J, Beveridge TJ (2003) Cryo-transmission electron
microscopy of frozen-hydrated sections of Escherichia coli and Pseudomonas aeruginosa.
J Bacteriol 185:6112–6118. https://doi.org/10.1128/JB.185.20.6112-6118.2003
148. Myers CR, Myers JM (2003) Cell surface exposure of the outer membrane cytochromes of
Shewanella oneidensis MR-1. Lett Appl Microbiol 37:254–258. https://doi.org/10.1046/j.
1472-765X.2003.01389.x
149. Myers JM, Myers CR (2001) Role for outer membrane cytochromes OmcA and OmcB of
Shewanella putrefaciens MR-1 in reduction of manganese dioxide. Appl Environ Microbiol
67:260–269. https://doi.org/10.1128/AEM.67.1.260
150. Zhang H, Tang X, Munske GR, Tolic N, Anderson GA, Bruce JE (2009) Identification of
protein-protein interactions and topologies in living cells with chemical cross-linking and
mass spectrometry. Mol Cell Proteomics 8:409–420. https://doi.org/10.1074/mcp.M800232MCP200
151. Shi L, Chen B, Wang Z, Elias DA, Mayer MU, Gorby YA, Ni S, Lower BH, Kennedy DW,
Wunschel DS, Mottaz HM, Marshall MJ, Hill EA, Beliaev AS, Zachara JM, Fredrickson JK,
Squier TC (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
152. Borloo J, Vergauwen B, De Smet L, Brigé A, Motte B, Devreese B, Van Beeumen J, De SL,
Brige A, Motte B, Devreese B, Van BJJ (2007) A kinetic approach to the dependence of
dissimilatory metal reduction by Shewanella oneidensis MR-1 on the outer membrane
cytochromes c OmcA and OmcB. FEBS J 274:3728–3738. https://doi.org/10.1111/j.17424658.2007.05907.x
153. Xiong Y, Shi L, Chen B, Mayer MU, Lower BH, Londer YY, Bose S, Hochella MF,
Fredrickson JK, Squier TC (2006) High-affinity binding and direct electron transfer to solid
metals by the Shewanella oneidensis MR-1 outer membrane c-type cytochrome OmcA.
J Am Chem Soc 128:13978–13979. https://doi.org/10.1021/ja063526d
154. Meitl LA, Eggleston CM, Colberg PJS, Khare N, Reardon CL, Shi L (2009) Electrochemical
interaction of Shewanella oneidensis MR-1 and its outer membrane cytochromes OmcA and
MtrC with hematite electrodes. Geochim Cosmochim Acta 73:5292–5307. https://doi.org/
10.1016/j.gca.2009.06.021
155. Eggleston CM, Vo J, Droubay TC, Colberg PJS (2008) Binding and direct electrochemistry
of OmcA, an outer-membrane cytochrome from an iron reducing bacterium, with oxide
electrodes: a candidate biofuel cell system. Inorganica Chim Acta 361:769–777. https://doi.
org/10.1016/j.ica.2007.07.015
156. Lower BH, Lins RD, Oestreicher Z, Straatsma TP, Hochella MF, Shi L, Lower SK (2008) In
vitro evolution of a peptide with a hematite binding motif that may constitute a natural
Bacterial Power: An Alternative Energy Source
243