112. Leys D, Tsapin AS, Nealson KH, Meyer TE, Cusanovich MA, Van BJJ, Van Beeumen JJ
(1999) Structure and mechanism of the flavocytochrome c fumarate reductase of Shewanella
putrefaciens MR-1. Nat Struct Biol 6:1113–1117. https://doi.org/10.1038/70051
113. Pessanha M, Rothery EL, Miles CS, Reid GA, Chapman SK, Louro RO, Turner DL,
Salgueiro CA, Xavier AV (2009) Tuning of functional heme reduction potentials in
Shewanella fumarate reductases. Biochim Biophys Acta 1787:113–120. https://doi.org/10.
1016/j.bbabio.2008.11.007
114. Paquete CM, Saraiva IH, Louro RO (2014) Redox tuning of the catalytic activity of soluble
fumarate reductases from Shewanella. Biochim Biophys Acta - Bioenerg 1837:717–725.
https://doi.org/10.1016/j.bbabio.2014.02.006
115. Alves MN, Fernandes AP, Salgueiro CA, Paquete CM (2016) Biochimica et Biophysica
Acta Unraveling the electron transfer processes of a nanowire protein from Geobacter
sulfurreducens. BBA - Bioenerg 1857:7–13. https://doi.org/10.1016/j.bbabio.2015.09.010
116. Tsapin AI, Nealson KH, Meyers T, Cusanovich MA, Van Beuumen J, Crosby LD,
Feinberg BA, Zhang C (1996) Purification and properties of a low-redox-potential tetraheme
cytochrome c 3 from Shewanella putrefaciens. J Bacteriol 178:6386–6388. https://doi.org/10.
1128/JB.178.21.6386-6388.1996
117. Coursolle D, Gralnick JA (2010) Modularity of the Mtr respiratory pathway of Shewanella
oneidensis
strain
MR-1.
Mol
Microbiol
1–14.
https://doi.org/10.1111/
j.1365-2958.2010.07266.x
118. Coursolle D, Gralnick JA (2012) Reconstruction of extracellular respiratory pathways for
iron(III) reduction in Shewanella oneidensis strain MR-1. Front Microbiol 3:1–11. https://
doi.org/10.3389/fmicb.2012.00056
119. Delgado VP, Paquete CM, Sturm G, Gescher J (2019) Improvement of the electron transfer
rate in Shewanella oneidensis MR-1 using a tailored periplasmic protein composition.
Bioelectrochemistry 129:18–25. https://doi.org/10.1016/j.bioelechem.2019.04.022
120. Leys D, Meyer TE, Tsapin AS, Nealson KH, Cusanovich MA, Van Beeumen JJ (2002)
Crystal structures at atomic resolution reveal the novel concept of “electron-harvesting” as a
role for the small tetraheme cytochrome c. J Biol Chem 277:35703–35711. https://doi.org/
10.1074/jbc.M203866200
121. Fonseca BM, Silva L, Trindade IB, Moe E, Matias PM, Louro RO, Paquete CM (2019)
Optimizing electroactive organisms: the effect of orthologous proteins. Front Energy Res
7:1–13. https://doi.org/10.3389/fenrg.2019.00002
122. Paixão VB, Salgueiro CA, Brennan L, Reid GA, Chapman SK, Turner DL (2008) The
solution structure of a tetraheme cytochrome from Shewanella frigidimarina reveals a novel
family structural motif. Biochemistry 47:11973–11980. https://doi.org/10.1021/bi801326j
123. Smith DMA, Rosso KM, Dupuis M, Valiev M, Straatsma TP (2006) Electronic coupling
between heme electron-transfer centers and its decay with distance depends strongly on
relative orientation. J Phys Chem B 110:15582–15588. https://doi.org/10.1021/jp057068r
124. Pessanha M, Louro RO, Correia IJIJ, Rothery EL, Pankhurst KLKL, Reid GA, Chapman SK,
Turner DL, Salgueiro CA (2003) Thermodynamic characterization of a tetrahaem
cytochrome isolated from a facultative aerobic bacterium, Shewanella frigidimarina : a
putative redox model for flavocytochrome c 3 . Biochem J 495:489–495. https://doi.org/10.
1042/BJ20021408
125. Fonseca BM, Saraiva IH, Paquete CM, Soares CM, Pacheco I, Salgueiro CA, Louro RO
(2009) The tetraheme cytochrome from Shewanella oneidensis MR-1 shows thermodynamic
bias for functional specificity of the hemes. J Biol Inorg Chem 14:375–385. https://doi.org/
10.1007/s00775-008-0455-7
126. Dolla A, Blanchard L, Guerlesquin F, Bruschi M (1994) The protein moiety modulates the
redox potential in cytochromes c. Biochimie 76:471–479. https://doi.org/10.1016/0300-9084
(94)90171-6
127. Martel PJ, Soares CM, Baptista AM, Fuxreiter M, Náray-Szabó G, Louro RO, Carrondo MA
(1999) Comparative redox and pK a calculations on cytochrome c 3 from several
Bacterial Power: An Alternative Energy Source
241
(1999) Structure and mechanism of the flavocytochrome c fumarate reductase of Shewanella
putrefaciens MR-1. Nat Struct Biol 6:1113–1117. https://doi.org/10.1038/70051
113. Pessanha M, Rothery EL, Miles CS, Reid GA, Chapman SK, Louro RO, Turner DL,
Salgueiro CA, Xavier AV (2009) Tuning of functional heme reduction potentials in
Shewanella fumarate reductases. Biochim Biophys Acta 1787:113–120. https://doi.org/10.
1016/j.bbabio.2008.11.007
114. Paquete CM, Saraiva IH, Louro RO (2014) Redox tuning of the catalytic activity of soluble
fumarate reductases from Shewanella. Biochim Biophys Acta - Bioenerg 1837:717–725.
https://doi.org/10.1016/j.bbabio.2014.02.006
115. Alves MN, Fernandes AP, Salgueiro CA, Paquete CM (2016) Biochimica et Biophysica
Acta Unraveling the electron transfer processes of a nanowire protein from Geobacter
sulfurreducens. BBA - Bioenerg 1857:7–13. https://doi.org/10.1016/j.bbabio.2015.09.010
116. Tsapin AI, Nealson KH, Meyers T, Cusanovich MA, Van Beuumen J, Crosby LD,
Feinberg BA, Zhang C (1996) Purification and properties of a low-redox-potential tetraheme
cytochrome c 3 from Shewanella putrefaciens. J Bacteriol 178:6386–6388. https://doi.org/10.
1128/JB.178.21.6386-6388.1996
117. Coursolle D, Gralnick JA (2010) Modularity of the Mtr respiratory pathway of Shewanella
oneidensis
strain
MR-1.
Mol
Microbiol
1–14.
https://doi.org/10.1111/
j.1365-2958.2010.07266.x
118. Coursolle D, Gralnick JA (2012) Reconstruction of extracellular respiratory pathways for
iron(III) reduction in Shewanella oneidensis strain MR-1. Front Microbiol 3:1–11. https://
doi.org/10.3389/fmicb.2012.00056
119. Delgado VP, Paquete CM, Sturm G, Gescher J (2019) Improvement of the electron transfer
rate in Shewanella oneidensis MR-1 using a tailored periplasmic protein composition.
Bioelectrochemistry 129:18–25. https://doi.org/10.1016/j.bioelechem.2019.04.022
120. Leys D, Meyer TE, Tsapin AS, Nealson KH, Cusanovich MA, Van Beeumen JJ (2002)
Crystal structures at atomic resolution reveal the novel concept of “electron-harvesting” as a
role for the small tetraheme cytochrome c. J Biol Chem 277:35703–35711. https://doi.org/
10.1074/jbc.M203866200
121. Fonseca BM, Silva L, Trindade IB, Moe E, Matias PM, Louro RO, Paquete CM (2019)
Optimizing electroactive organisms: the effect of orthologous proteins. Front Energy Res
7:1–13. https://doi.org/10.3389/fenrg.2019.00002
122. Paixão VB, Salgueiro CA, Brennan L, Reid GA, Chapman SK, Turner DL (2008) The
solution structure of a tetraheme cytochrome from Shewanella frigidimarina reveals a novel
family structural motif. Biochemistry 47:11973–11980. https://doi.org/10.1021/bi801326j
123. Smith DMA, Rosso KM, Dupuis M, Valiev M, Straatsma TP (2006) Electronic coupling
between heme electron-transfer centers and its decay with distance depends strongly on
relative orientation. J Phys Chem B 110:15582–15588. https://doi.org/10.1021/jp057068r
124. Pessanha M, Louro RO, Correia IJIJ, Rothery EL, Pankhurst KLKL, Reid GA, Chapman SK,
Turner DL, Salgueiro CA (2003) Thermodynamic characterization of a tetrahaem
cytochrome isolated from a facultative aerobic bacterium, Shewanella frigidimarina : a
putative redox model for flavocytochrome c 3 . Biochem J 495:489–495. https://doi.org/10.
1042/BJ20021408
125. Fonseca BM, Saraiva IH, Paquete CM, Soares CM, Pacheco I, Salgueiro CA, Louro RO
(2009) The tetraheme cytochrome from Shewanella oneidensis MR-1 shows thermodynamic
bias for functional specificity of the hemes. J Biol Inorg Chem 14:375–385. https://doi.org/
10.1007/s00775-008-0455-7
126. Dolla A, Blanchard L, Guerlesquin F, Bruschi M (1994) The protein moiety modulates the
redox potential in cytochromes c. Biochimie 76:471–479. https://doi.org/10.1016/0300-9084
(94)90171-6
127. Martel PJ, Soares CM, Baptista AM, Fuxreiter M, Náray-Szabó G, Louro RO, Carrondo MA
(1999) Comparative redox and pK a calculations on cytochrome c 3 from several
Bacterial Power: An Alternative Energy Source
241