Unfolding cytochromes c-b562 and Rd apo b562

ABSTRACT Two abundant, low-redox-potential cytochromesc were purified from the facultative anaerobeShewanella 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 fromShewanella frigidimarina (formerly Shewanella putrefaciens) NCIMB400 and the unclassified bacterial strain H1R (64 and 55% identity, respectively). The amount of the small tetraheme cytochrome is regulated by anaerobiosis, but not by fumarate. The larger of the two low-potential cytochromes contains tetraheme and flavin domains and is regulated by anaerobiosis and by fumarate and thus most nearly corresponds to the flavocytochromec-fumarate reductase previously characterized fromS. frigidimarina to which it is 59% identical. However, the genetic context of the cytochrome genes is not the same for the twoShewanella species, and they are not located in multicistronic operons. The small cytochrome c and the cytochrome domain of the flavocytochrome c are also homologous, showing 34% identity. Structural comparison shows that theShewanella tetraheme cytochromes are not related to theDesulfovibrio cytochromes c 3but define a new folding motif for small multiheme cytochromesc.

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Structures of Various Cytochromes c Evaluated from the Redox Behaviors Using the Optically Active Co(III) Complex-Modified Au Electrode

Drug Metabolism Letters ◽

10.2174/187231207779814265 ◽

2007 ◽

Vol 1 (1) ◽

pp. 73-75

Author(s):

Isao Takahashi ◽

Chika Nishijima ◽

Tomohiko Inomata ◽

Yasuhiro Funahashi ◽

Tomohiro Ozawa ◽

...

Keyword(s):

Optically Active ◽

Au Electrode ◽

Cytochromes C

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The metal reductase activity of some multiheme cytochromes c: NMR structural characterization of the reduction of chromium(VI) to chromium(III) by cytochrome c7

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.152290999 ◽

2002 ◽

Vol 99 (15) ◽

pp. 9750-9754 ◽

Cited By ~ 32

Author(s):

M. Assfalg ◽

I. Bertini ◽

M. Bruschi ◽

C. Michel ◽

P. Turano

Keyword(s):

Structural Characterization ◽

Reductase Activity ◽

Chromium Vi ◽

Cytochromes C ◽

Cytochrome C7 ◽

C Nmr

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Purification and properties of the soluble cytochromes c-550 and c-556 from the bacterium Aquaspirillum itersonii

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1987.tb13491.x ◽

1987 ◽

Vol 166 (1) ◽

pp. 127-130 ◽

Cited By ~ 1

Author(s):

Kevin J. WOOLLEY

Keyword(s):

Purification And Properties ◽

Cytochromes C

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The amino acid sequence of cytochromes c-551 from three species of Pseudomonas

Biochemical Journal ◽

10.1042/bj1310485 ◽

1973 ◽

Vol 131 (3) ◽

pp. 485-498 ◽

Cited By ~ 113

Author(s):

R. P. Ambler ◽

Margaret Wynn

Keyword(s):

Amino Acids ◽

Pseudomonas Aeruginosa ◽

Amino Acid ◽

Cytochrome C ◽

Amino Acid Sequence ◽

Amino Acid Sequences ◽

Mitochondrial Cytochrome ◽

Cytochromes C ◽

Lending Library ◽

Single Peptide

The amino acid sequences of the cytochromes c-551 from three species of Pseudomonas have been determined. Each resembles the protein from Pseudomonas strain P6009 (now known to be Pseudomonas aeruginosa, not Pseudomonas fluorescens) in containing 82 amino acids in a single peptide chain, with a haem group covalently attached to cysteine residues 12 and 15. In all four sequences 43 residues are identical. Although by bacteriological criteria the organisms are closely related, the differences between pairs of sequences range from 22% to 39%. These values should be compared with the differences in the sequence of mitochondrial cytochrome c between mammals and amphibians (about 18%) or between mammals and insects (about 33%). Detailed evidence for the amino acid sequences of the proteins has been deposited as Supplementary Publication SUP 50015 at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1973), 131, 5.

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