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MtrC, an outer membrane decahaem c cytochrome required for metal reduction in Shewanella putrefaciens MR‐1
Author(s) -
Beliaev Alex S.,
Saffarini Daad A.,
McLaughlin Jennifer L.,
Hunnicutt David
Publication year - 2001
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.2001.02257.x
Subject(s) - periplasmic space , shewanella putrefaciens , biology , cytochrome , reductase , shewanella , bacterial outer membrane , biochemistry , cytochrome c , electron transport chain , shewanella oneidensis , heme , mutant , anaerobic respiration , bacteria , enzyme , mitochondrion , escherichia coli , genetics , gene
Shewanella putrefaciens is a facultative anaerobe that can use metal oxides as terminal electron acceptors during anaerobic respiration. Two proteins, MtrB and Cct, have been identified that are specifically involved in metal reduction. Analysis of S. putrefaciens mutants deficient in metal reduction led to the identification of two additional proteins that are involved in this process. MtrA is a periplasmic decahaem c ‐type cytochrome that appears to be part of the electron transport chain, which leads to Fe(III) and Mn(IV) reduction. MtrC is an outer membrane decahaem c ‐type cytochrome that appears to be required for the activity of the terminal Fe(III) reductase. Membrane fractions of mutants deficient in MtrC exhibited a decreased level of Fe(III) reduction compared with the wild type. We suggest that MtrC may be a component of the terminal reductase or may be required for its assembly.