4.5 Article

QcrCAB operon of a nocardia-form actinomycete Rhodococcus rhodochrous encodes cytochrome reductase complex with diheme cytochrome cc subunit

Journal

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
Volume 1557, Issue 1-3, Pages 125-131

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ELSEVIER
DOI: 10.1016/S0005-2728(02)00394-8

Keywords

quinol-cytochrome c reductase; cytochrome cc; Rieske Fe-S protein; cytochrome b; Rhodococcus rhodochrous

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Structural genes encoding quinol-cytochrome c reductase (QcR) were cloned and sequenced from nocardia-form actinomycete Rhodococcus rhodochrous. QcrC and qcrA encode diheme cytochrome cc and the Rieske Fe-S protein, respectively, while the qcrB product is a diheme cytochrome b. These amino acid sequences are similar to those of Corynebacterium and Mycobacterium, the members of high G+C content firmicutes. The presence of diheme cytochrome cc subunit as a sole c-type cytochrome in these organisms suggests the direct elecron transfer to cytochrome c oxidase. The N-terminal half of the Rieske Fe-S proteins of these bacteria has a unique structure with three transmembrane helices, while the C-terminal half sequence is conserved. A phylogenetic tree using the latter region showed that high G+C firmicutes form a clear clade with Thermus, but not with low G+C firmicutes. (C) 2002 Elsevier Science B.V. All rights reserved.

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