1887

Abstract

Spectroscopic analysis of membranes isolated from , along with analysis of its genome, indicates that the cytochrome branch of its respiratory pathway consists of a modified complex that contains two cytochromes in its subunit, similar to other acid-fast bacteria, and an -type cytochrome oxidase. A functional association of the cytochrome and complexes was indicated by the findings that levels of detergent sufficient to completely disrupt isolated membranes failed to inhibit quinol-driven O reduction, but known inhibitors of the complex did inhibit quinol-driven O reduction. The gene for subunit II of the -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 O reduction, suggesting that ionic interactions between extramembrane domains do not play the major role in stabilizing the interaction. Divalent cations did inhibit electron transfer, likely by distorting the electron-transfer interface between cytochrome and subunit II. Soluble cytochrome cannot donate electrons to the -type oxidase, even though key cytochrome -binding residues are conserved, probably because the additional residues of subunit II prevent the binding of soluble cytochrome . The results indicate that hydrophobic interactions are the primary forces maintaining the interaction, but ionic interactions may assist in aligning the two complexes for efficient electron transfer.

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2006-03-01
2019-11-14
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