genes in the Shewanella oneidensis genome and characterization of six soluble cytochromes.
Omi A J Integr Biol 8:57–77. https://doi.org/10.1089/153623104773547499
82. Bretschger O, Obraztsova A, Sturm CA, Chang IS, Gorby YA, Reed SB, Culley DE,
Reardon CL, Barua S, Romine MF, Zhou J, Beliaev AS, Bouhenni R, Saffarini D,
Mansfeld F, Kim B-H, Fredrickson JK, Nealson KH (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
83. Rosenbaum MA, Bar HY, Beg QK, Segrè D, Booth J, Cotta MA, Angenent LT (2012)
Transcriptional analysis of Shewanella oneidensis MR-1 with an electrode compared to Fe
(III)citrate or oxygen as terminal electron acceptor. PLoS One 7:e30827. https://doi.org/10.
1371/journal.pone.0030827
84. Richardson D (2002) PMF through the redox loop. Science 295:1842–1843. https://doi.org/
10.1126/science.1070366
85. Scott JH, Nealson KH (1994) A biochemical study of the intermediary carbon metabolism of
Shewanella putrefaciens. J Bacteriol 176:3408–3411. https://doi.org/10.1128/JB.176.11.
3408-3411.1994
86. Hunt KA, Flynn JM, Naranjo B, Shikhare ID, Gralnick JA (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
87. Myers CR, Myers JM (1993b) Role of menaquinone in the reduction of fumarate, nitrate,
iron(III) and manganese(IV) by Shewanella putrefaciens MR-1. FEMS Microbiol Lett
114:215–222. https://doi.org/10.1111/j.1574-6968.1993.tb06576.x
88. Marritt SJ, McMillan DGG, Shi L, Fredrickson JK, Zachara JM, Richardson DJ,
Jeuken LJC, Butt JN (2012) The roles of CymA in support of the respiratory flexibility of
Shewanella oneidensis MR-1. Biochem Soc Trans 40:1217–1221. https://doi.org/10.1042/
bst20120150
89. Saffarini DA, Blumerman SL, Mansoorabadi KJ (2002) Role of Menaquinones in Fe
(III) reduction by membrane fractions of Shewanella putrefaciens. J Bacteriol 184:846–848.
https://doi.org/10.1128/JB.184.3.846
90. Myers CR, Myers JM (1997) Cloning and sequence of cymA, a gene encoding a tetraheme
cytochrome C required for reduction of Iron (III), fumarate, and nitrate by Shewanella
putrefaciens MR-1. J Bacteriol 179:1143–1152. https://doi.org/10.1128/jb.179.4.1143-1152.
1997
91. Myers JM, Myers CR (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
92. Schwalb C, Chapman SK, Reid GA (2002) The membrane-bound tetrahaem c -type
cytochrome CymA interacts directly with the soluble fumarate reductase in Shewanella.
Biochem Soc Trans 30:658–662. https://doi.org/10.1042/bst0300658
93. Zhong Y, Shi L (2018) Genomic analyses of the quinol oxidases and/or quinone reductases
involved in bacterial extracellular electron transfer. Front Microbiol 9:1–12. https://doi.org/
10.3389/fmicb.2018.03029
94. Zargar K, Saltikov CW (2009) Lysine-91 of the tetraheme c-type cytochrome CymA is
essential for quinone interaction and arsenate respiration in Shewanella sp. Arch Microbiol
191:797–806. https://doi.org/10.1007/s00203-009-0511-x
95. Field SJ, Dobbin PS, Cheesman MR, Watmough NJ, Thomson AJ, Richardson DJ (2000)
Purification and magneto-optical spectroscopic characterization of cytoplasmic membrane
and outer membrane multiheme c-type cytochromes from Shewanella frigidimarina
NCIMB400. J Biol Chem 275:8515–8522. https://doi.org/10.1074/jbc.275.12.8515
96. Firer-Sherwood MA, Bewley KD, Mock JY, Elliott SJ (2011) Tools for resolving
complexity in the electron transfer networks of multiheme cytochromes c. Metallomics
3:344–348. https://doi.org/10.1039/c0mt00097c
Bacterial Power: An Alternative Energy Source
239
Omi A J Integr Biol 8:57–77. https://doi.org/10.1089/153623104773547499
82. Bretschger O, Obraztsova A, Sturm CA, Chang IS, Gorby YA, Reed SB, Culley DE,
Reardon CL, Barua S, Romine MF, Zhou J, Beliaev AS, Bouhenni R, Saffarini D,
Mansfeld F, Kim B-H, Fredrickson JK, Nealson KH (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
83. Rosenbaum MA, Bar HY, Beg QK, Segrè D, Booth J, Cotta MA, Angenent LT (2012)
Transcriptional analysis of Shewanella oneidensis MR-1 with an electrode compared to Fe
(III)citrate or oxygen as terminal electron acceptor. PLoS One 7:e30827. https://doi.org/10.
1371/journal.pone.0030827
84. Richardson D (2002) PMF through the redox loop. Science 295:1842–1843. https://doi.org/
10.1126/science.1070366
85. Scott JH, Nealson KH (1994) A biochemical study of the intermediary carbon metabolism of
Shewanella putrefaciens. J Bacteriol 176:3408–3411. https://doi.org/10.1128/JB.176.11.
3408-3411.1994
86. Hunt KA, Flynn JM, Naranjo B, Shikhare ID, Gralnick JA (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
87. Myers CR, Myers JM (1993b) Role of menaquinone in the reduction of fumarate, nitrate,
iron(III) and manganese(IV) by Shewanella putrefaciens MR-1. FEMS Microbiol Lett
114:215–222. https://doi.org/10.1111/j.1574-6968.1993.tb06576.x
88. Marritt SJ, McMillan DGG, Shi L, Fredrickson JK, Zachara JM, Richardson DJ,
Jeuken LJC, Butt JN (2012) The roles of CymA in support of the respiratory flexibility of
Shewanella oneidensis MR-1. Biochem Soc Trans 40:1217–1221. https://doi.org/10.1042/
bst20120150
89. Saffarini DA, Blumerman SL, Mansoorabadi KJ (2002) Role of Menaquinones in Fe
(III) reduction by membrane fractions of Shewanella putrefaciens. J Bacteriol 184:846–848.
https://doi.org/10.1128/JB.184.3.846
90. Myers CR, Myers JM (1997) Cloning and sequence of cymA, a gene encoding a tetraheme
cytochrome C required for reduction of Iron (III), fumarate, and nitrate by Shewanella
putrefaciens MR-1. J Bacteriol 179:1143–1152. https://doi.org/10.1128/jb.179.4.1143-1152.
1997
91. Myers JM, Myers CR (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
92. Schwalb C, Chapman SK, Reid GA (2002) The membrane-bound tetrahaem c -type
cytochrome CymA interacts directly with the soluble fumarate reductase in Shewanella.
Biochem Soc Trans 30:658–662. https://doi.org/10.1042/bst0300658
93. Zhong Y, Shi L (2018) Genomic analyses of the quinol oxidases and/or quinone reductases
involved in bacterial extracellular electron transfer. Front Microbiol 9:1–12. https://doi.org/
10.3389/fmicb.2018.03029
94. Zargar K, Saltikov CW (2009) Lysine-91 of the tetraheme c-type cytochrome CymA is
essential for quinone interaction and arsenate respiration in Shewanella sp. Arch Microbiol
191:797–806. https://doi.org/10.1007/s00203-009-0511-x
95. Field SJ, Dobbin PS, Cheesman MR, Watmough NJ, Thomson AJ, Richardson DJ (2000)
Purification and magneto-optical spectroscopic characterization of cytoplasmic membrane
and outer membrane multiheme c-type cytochromes from Shewanella frigidimarina
NCIMB400. J Biol Chem 275:8515–8522. https://doi.org/10.1074/jbc.275.12.8515
96. Firer-Sherwood MA, Bewley KD, Mock JY, Elliott SJ (2011) Tools for resolving
complexity in the electron transfer networks of multiheme cytochromes c. Metallomics
3:344–348. https://doi.org/10.1039/c0mt00097c
Bacterial Power: An Alternative Energy Source
239