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. 1991 Jul 15;88(14):6122–6126. doi: 10.1073/pnas.88.14.6122

The heme groups of cytochrome o from Escherichia coli.

A Puustinen 1, M Wikström 1
PMCID: PMC52034  PMID: 2068092

Abstract

Cytochrome o, one of the two terminal ubiquinol oxidases of Escherichia coli, is structurally and functionally related to cytochrome c oxidase of mitochondria and some bacteria. It has two heme groups, one of which binds CO and forms a binuclear oxygen reaction center with copper. The other heme is unreactive toward ligands, exhibits strong interactions with the binuclear center, and is mainly responsible for the reduced-minus-oxidized alpha band. Protoheme has been thought to be the prosthetic group of b-type cytochromes, including cytochrome o. However, the hemes of cytochrome o are of a different kind, for which we propose the name heme O. Its pyridine hemochrome spectrum is blue-shifted by 4 nm relative to that of protoheme, and chromatographic behavior showed that it is much more hydrophobic than protoheme. Fast atom bombardment mass spectrometry yielded a molecular mass of 839 Da. Heme O is proposed to be a heme A-like molecule, containing a 17-carbon hydroxyethylfarnesyl side chain, but with a methyl residue replacing the formyl group.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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