97. Fonseca BM, Paquete CM, Neto SE, Pacheco I, Soares CM, Louro RO (2013) Mind the gap:
cytochrome interactions reveal electron pathways across the periplasm of Shewanella
oneidensis MR-1. Biochem J 449:101–108
98. Vellingiri A, Song YE, Munussami G, Kim C, Park C, Jeon B-H, Lee S-G, Kim JR (2019)
Overexpression of c-type cytochrome, CymA in Shewanella oneidensis MR-1 for enhanced
bioelectricity generation and cell growth in a microbial fuel cell. J Chem Technol Biotechnol
94:2115–2122. https://doi.org/10.1002/jctb.5813
99. Gescher J, Cordova CD, Spormann AM (2008) Dissimilatory iron reduction in Escherichia
coli: identification of CymA of Shewanella oneidensis and NapC of E. coli as ferric
reductases. Mol Microbiol 68:706–719. https://doi.org/10.1111/j.1365-2958.2008.06183.x
100. Louro RO, Paquete CM (2012) The quest to achieve the detailed structural and functional
characterization of CymA. Biochem Soc Trans 40:1291–1294. https://doi.org/10.1042/
bst20120114
101. Firer-Sherwood M, Su Pulcu G, J. Elliott S, (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
102. Cordova CD, Schicklberger MFR, Yu Y, Spormann AM (2011) Partial functional
replacement of CymA by SirCD in Shewanella oneidensis MR-1. J Bacteriol 193:2312–
2321. https://doi.org/10.1128/JB.01355-10
103. Breuer M, Rosso KM, Blumberger J, Butt JN (2015) Multi-haem cytochromes in
Shewanella oneidensis MR-1: structures, functions and opportunities. J R Soc Interface
12. https://doi.org/10.1098/rsif.2014.1117
104. Lemaire ON, Honoré FA, Jourlin-Castelli C, Méjean V, Fons M, Iobbi-Nivol C (2016)
Efficient respiration on TMAO requires TorD and TorE auxiliary proteins in Shewanella
oneidensis. Res Microbiol 167:630–637. https://doi.org/10.1016/j.resmic.2016.05.004
105. Dohnalkova AC, Marshall MJ, Arey BW, Williams KH, Buck EC, Fredrickson JK (2011)
Imaging hydrated microbial extracellular polymers: Comparative analysis by electron
microscopy. Appl Environ Microbiol 77:1254–1262. https://doi.org/10.1128/AEM.0200110
106. Sturm G, Richter K, Doetsch A, Heide H, Louro RO, 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
107. Tsapin AI, Vandenberghe I, Nealson KH, Scott JH, Meyer TE, Cusanovich MA, Harada E,
Kaizu T, Akutsu H, Leys D, Van BJJ (2001) Identification of a small tetraheme cytochrome
c and a flavocytochrome c as two of the principal soluble cytochromes c in Shewanella
oneidensis strain MR1. Appl Environ Microbiol 67:3236–3244. https://doi.org/10.1128/
AEM.67.7.3236
108. Schuetz B, Schicklberger M, Kuermann J, Spormann AM, Gescher J, Kuermann J,
Spormann AM, Gescher J (2009) Periplasmic electron transfer via the c-type cytochromes
Mtra and Fcca of Shewanella oneidensis Mr-1. Appl Environ Microbiol 75:7789–7796.
https://doi.org/10.1128/AEM.01834-09
109. Gordon EHJ, Pike AD, Hill AE, Cuthbertson PM, Chapman SK, Reid GA (2000)
Identification and characterization of a novel cytochrome c 3 from Shewanella frigidimarina
that is involved in Fe(III) respiration. Biochem J 349:153–158. https://doi.org/10.1042/02646021:3490153
110. Pealing SL, Black AC, Manson FDC, Ward FB, Chapman SK, Reid GA (1992) Sequence of
the gene encoding flavocytochrome. Biochemistry 31:12132–12140. https://doi.org/10.1021/
bi00163a023
111. Taylor P, Pealing SL, Reid GA, Chapman SK, Walkinshaw MD (1999) Structural and
mechanistic mapping of a unique fumarate reductase. Nat Struct Biol 6:1108–1112. https://
doi.org/10.1038/70045
240
B. M. Fonseca et al.
cytochrome interactions reveal electron pathways across the periplasm of Shewanella
oneidensis MR-1. Biochem J 449:101–108
98. Vellingiri A, Song YE, Munussami G, Kim C, Park C, Jeon B-H, Lee S-G, Kim JR (2019)
Overexpression of c-type cytochrome, CymA in Shewanella oneidensis MR-1 for enhanced
bioelectricity generation and cell growth in a microbial fuel cell. J Chem Technol Biotechnol
94:2115–2122. https://doi.org/10.1002/jctb.5813
99. Gescher J, Cordova CD, Spormann AM (2008) Dissimilatory iron reduction in Escherichia
coli: identification of CymA of Shewanella oneidensis and NapC of E. coli as ferric
reductases. Mol Microbiol 68:706–719. https://doi.org/10.1111/j.1365-2958.2008.06183.x
100. Louro RO, Paquete CM (2012) The quest to achieve the detailed structural and functional
characterization of CymA. Biochem Soc Trans 40:1291–1294. https://doi.org/10.1042/
bst20120114
101. Firer-Sherwood M, Su Pulcu G, J. Elliott S, (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
102. Cordova CD, Schicklberger MFR, Yu Y, Spormann AM (2011) Partial functional
replacement of CymA by SirCD in Shewanella oneidensis MR-1. J Bacteriol 193:2312–
2321. https://doi.org/10.1128/JB.01355-10
103. Breuer M, Rosso KM, Blumberger J, Butt JN (2015) Multi-haem cytochromes in
Shewanella oneidensis MR-1: structures, functions and opportunities. J R Soc Interface
12. https://doi.org/10.1098/rsif.2014.1117
104. Lemaire ON, Honoré FA, Jourlin-Castelli C, Méjean V, Fons M, Iobbi-Nivol C (2016)
Efficient respiration on TMAO requires TorD and TorE auxiliary proteins in Shewanella
oneidensis. Res Microbiol 167:630–637. https://doi.org/10.1016/j.resmic.2016.05.004
105. Dohnalkova AC, Marshall MJ, Arey BW, Williams KH, Buck EC, Fredrickson JK (2011)
Imaging hydrated microbial extracellular polymers: Comparative analysis by electron
microscopy. Appl Environ Microbiol 77:1254–1262. https://doi.org/10.1128/AEM.0200110
106. Sturm G, Richter K, Doetsch A, Heide H, Louro RO, 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
107. Tsapin AI, Vandenberghe I, Nealson KH, Scott JH, Meyer TE, Cusanovich MA, Harada E,
Kaizu T, Akutsu H, Leys D, Van BJJ (2001) Identification of a small tetraheme cytochrome
c and a flavocytochrome c as two of the principal soluble cytochromes c in Shewanella
oneidensis strain MR1. Appl Environ Microbiol 67:3236–3244. https://doi.org/10.1128/
AEM.67.7.3236
108. Schuetz B, Schicklberger M, Kuermann J, Spormann AM, Gescher J, Kuermann J,
Spormann AM, Gescher J (2009) Periplasmic electron transfer via the c-type cytochromes
Mtra and Fcca of Shewanella oneidensis Mr-1. Appl Environ Microbiol 75:7789–7796.
https://doi.org/10.1128/AEM.01834-09
109. Gordon EHJ, Pike AD, Hill AE, Cuthbertson PM, Chapman SK, Reid GA (2000)
Identification and characterization of a novel cytochrome c 3 from Shewanella frigidimarina
that is involved in Fe(III) respiration. Biochem J 349:153–158. https://doi.org/10.1042/02646021:3490153
110. Pealing SL, Black AC, Manson FDC, Ward FB, Chapman SK, Reid GA (1992) Sequence of
the gene encoding flavocytochrome. Biochemistry 31:12132–12140. https://doi.org/10.1021/
bi00163a023
111. Taylor P, Pealing SL, Reid GA, Chapman SK, Walkinshaw MD (1999) Structural and
mechanistic mapping of a unique fumarate reductase. Nat Struct Biol 6:1108–1112. https://
doi.org/10.1038/70045
240
B. M. Fonseca et al.