Abstract:
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.
journal_name
Lett Appl Microbioljournal_title
Letters in applied microbiologyauthors
Myers JM,Myers CRdoi
10.1046/j.1472-765x.2003.01338.xsubject
Has Abstractpub_date
2003-01-01 00:00:00pages
21-5issue
1eissn
0266-8254issn
1472-765Xpii
1338journal_volume
37pub_type
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journal_title:Letters in applied microbiology
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doi:10.1111/j.1472-765x.1996.tb00195.x
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pub_type: 杂志文章
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