Structural and Functional Studies of Multiheme Cytochromes c Involved in Extracellular Electron Transport in Bacterial Dissimilatory Metal Reduction

被引:7
|
作者
Tikhonova, T. V. [1 ]
Popov, V. O. [1 ]
机构
[1] Russian Acad Sci, Bach Inst Biochem, Moscow 119071, Russia
基金
俄罗斯基础研究基金会;
关键词
bacterial dissimilatory metal reduction; extracellular electron transfer; multiheme cytochrome c; OUTER-MEMBRANE CYTOCHROMES; SHEWANELLA-PUTREFACIENS MR-1; FE(III) OXIDE REDUCTION; CRYSTAL-STRUCTURE; IRON REDUCTION; DECAHEME CYTOCHROME; RESPIRATORY FLEXIBILITY; ANAEROBIC RESPIRATION; MICROBIAL NANOWIRES; FUMARATE REDUCTASE;
D O I
10.1134/S0006297914130094
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Bacteria utilizing insoluble mineral forms of metal oxides as electron acceptors in respiratory processes are wide-spread in the nature. The electron transfer from a pool of reduced quinones in the cytoplasmic membrane across the periplasm to the bacterial outer membrane and then to an extracellular acceptor is a key step in bacterial dissimilatory metal reduction. Multiheme cytochromes c play a crucial role in the extracellular electron transfer. The bacterium Shewanella oneidensis MR-1 was used as a model organism to study the mechanism of extracellular electron transport. In this review, we discuss recent data on the composition, structures, and functions of multiheme cytochromes c and their functional complexes responsible for extracellular electron transport in Shewanella oneidensis.
引用
收藏
页码:1584 / 1601
页数:18
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