Purification and properties of a low-redox-potential tetraheme cytochrome c3 from Shewanella putrefaciens

Author:

Tsapin A I1,Nealson K H1,Meyers T1,Cusanovich M A1,Van Beuumen J1,Crosby L D1,Feinberg B A1,Zhang C1

Affiliation:

1. Center for Great Lakes Studies and Department of Chemistry, University of Wisconsin-Milwaukee, USA.

Abstract

Shewanella putrefaciens is a facultatively anaerobic bacterium in the gamma group of the proteobacteria, capable of utilizing a wide variety of anaerobic electron acceptors. An examination of its cytochrome content revealed the presence of a tetraheme, low-redox-potential (E'o = -233 mV), cytochrome c-type cytochrome with a molecular mass of 12,120 Da and a pI of 5.8. The electron spin resonance data indicate a bis-histidine coordination of heme groups. Reduction of ferric citrate was accompanied by oxidation of the cytochrome. The biochemical properties suggested that this protein was in the cytochrome c3 group, which is supported by N-terminal sequence data up to the first heme binding site.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

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5. Lies D. D. Moser H. Sano M. Nishijima and M. Sakai. 1996. Types and levels of isoprenoid quinones synthesized under various growth conditions for strains of Shewanella putrefaciens abstr. K-72 p. 104. In Abstracts of the 96th General Meeting of the American Society for Microbiology 1996. American Society for Microbiology Washington D.C.

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