Evidence for a cytochrome bcc-aa3 interaction in the respiratory chain of Mycobacterium smegmatis

Microbiology
James A MegeheeMichael D Lundrigan

Abstract

Spectroscopic analysis of membranes isolated from Mycobacterium smegmatis, along with analysis of its genome, indicates that the cytochrome c branch of its respiratory pathway consists of a modified bc1 complex that contains two cytochromes c in its c1 subunit, similar to other acid-fast bacteria, and an aa3-type cytochrome c oxidase. A functional association of the cytochrome bcc and aa3 complexes was indicated by the findings that levels of detergent sufficient to completely disrupt isolated membranes failed to inhibit quinol-driven O2 reduction, but known inhibitors of the bc1 complex did inhibit quinol-driven O2 reduction. The gene for subunit II of the aa3-type oxidase indicates the presence of additional charged residues in a predicted extramembrane domain, which could mediate an intercomplex association. However, high concentrations of monovalent salts had no effect on O2 reduction, suggesting that ionic interactions between extramembrane domains do not play the major role in stabilizing the bcc-aa3 interaction. Divalent cations did inhibit electron transfer, likely by distorting the electron-transfer interface between cytochrome c1 and subunit II. Soluble cytochrome c cannot donate electrons to the aa3-type oxidase, eve...Continue Reading

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Citations

Mar 23, 2012·The Journal of Biological Chemistry·Sanjay GuptaKanak L Dikshit
Jun 1, 2007·Canadian Journal of Microbiology·James A Megehee, Michael D Lundrigan
Nov 8, 2015·Biochimica Et Biophysica Acta·Axel Magalon, François Alberge
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