Journal
LETTERS IN APPLIED MICROBIOLOGY
Volume 37, Issue 1, Pages 21-25Publisher
BLACKWELL PUBLISHING LTD
DOI: 10.1046/j.1472-765X.2003.01338.x
Keywords
cytochrome; OmcA; OmcB; outer membrane; Shewanella oneidensis
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Funding
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM050786] Funding Source: NIH RePORTER
- NIGMS NIH HHS [R01GM50786] Funding Source: Medline
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Aim: To determine if the outer membrane (OM) cytochromes OmcA and OmcB of the metal-reducing bacterium Shewanella oneidensis MR-1 have distinct or overlapping roles in the reduction of insoluble manganese(IV) oxide. Methods and Results: The gene replacement mutant (OMCA1) which lacks OmcA was partially deficient in Mn(IV) reduction. Complementation of OMCA1 with a vector (pVK21) that contains omcB but not omcA restored Mn(IV) reduction to levels that were even greater than those of wild-type. Examination of the OM of OMCA1/pVK21 revealed greater than wild-type levels of OmcB protein and specific haem content. Conclusions: Overexpression of OmcB can compensate for the absence of OmcA in the reduction of insoluble Mn(IV) oxides. Therefore, there is at least a partial overlap in the roles of these OM cytochromes in the reduction of insoluble Mn(IV) oxide. Significance: The overlapping roles of these two cytochromes has important implications for understanding the mechanism by which MR-1 reduces insoluble metal oxides. There is no obligatory sequential electron transfer from one cytochrome to the other. They could both potentially serve as terminal reductases for extracellular electron acceptors.
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