Structure and function of flavocytochrome c3, the soluble fumarate reductase from Shewanella NCIMB400.
نویسندگان
چکیده
418 Structure and function of flavocytochrome c3, the soluble fumarate reductase from Shewanella NCI M 6400 G. A. Reid*', E. H. J. Gordon*', A. E. Hill*, M. Dohertyt, K. Turnert, R. Halt* and S. K. Chapmant *Institute of Cell and Molecular Biology and tDepartment of Chemistry, University of Edinburgh, Mayfield Road, Edinburgh EH9 3]R, Scotland, U.K., and SZeneca Life Science Molecules, Belasis Avenue, Billingham TS23 I YN, U.K.
منابع مشابه
Identification of a small tetraheme cytochrome c and a flavocytochrome c as two of the principal soluble cytochromes c in Shewanella oneidensis strain MR1.
Two abundant, low-redox-potential cytochromes c were purified from the facultative anaerobe Shewanella oneidensis strain MR1 grown anaerobically with fumarate. The small cytochrome was completely sequenced, and the genes coding for both proteins were cloned and sequenced. The small cytochrome c contains 91 residues and four heme binding sites. It is most similar to the cytochromes c from Shewan...
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Respiratory and photosynthetic electron transfer chains are dependent on vectorial electron transfer through a series of redox proteins. Examples include electron transfer from NapC to NapAB nitrate reductase in Paracoccus denitrificans and from CymA to Fcc3 (flavocytochrome c3) fumarate reductase in Shewanella oneidensis MR-1. In the present article, we demonstrate that graphite electrodes can...
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Protein-protein interactions are well-known to regulate enzyme activity in cell signaling and metabolism. Here, we show that protein-protein interactions regulate the activity of a respiratory-chain enzyme, CymA, by changing the direction or bias of catalysis. CymA, a member of the widespread NapC/NirT superfamily, is a menaquinol-7 (MQ-7) dehydrogenase that donates electrons to several distinc...
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ورودعنوان ژورنال:
- Biochemical Society transactions
دوره 26 3 شماره
صفحات -
تاریخ انتشار 1998