PMID: 9171438Jun 1, 1997Paper

Formation of pH and potential gradients by the reconstituted Azotobacter vinelandii cytochrome bd respiratory protection oxidase

Journal of Bacteriology
J F Kolonay, R J Maier

Abstract

To directly characterize the bioenergetic properties of the cytochrome bd terminating branch of the Azotobacter vinelandii electron transport chain, the purified cytochrome bd oxidase was reconstituted into a phospholipid environment consisting of phosphatidylethanolamine and phosphatidylglycerol (3:1). The average diameter of the proteoliposomes after extrusion through a polycarbonate membrane was 94 +/- 4 nm. Initiation of respiration upon the addition of 20 microM ubiquinone-1 to proteoliposomes loaded with the pH-sensitive dye pyranine resulted in an immediate alkalization of the vesicle lumen by an average pH change of 0.11 unit. This pH gradient was readily collapsed upon the addition of nigericin, carbonyl cyanide p-(tri-fluoromethoxy) phenyl-hydrazone, gramicidin, Triton X-100, or 2-heptyl-4-hydroxyquinoline N-oxide (HQNO). Proteoliposomal respiration initiated in the presence of the potentiometric membrane dye rhodamine 123 caused the generation of a transmembrane potential; the potential was collapsed upon the addition of either valinomycin or HQNO. The formation of both pH and potential gradients during turnover demonstrates that the A. vinelandii cytochrome bd oxidase is coupled to energy conservation in vivo.

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Citations

Feb 25, 2005·Proceedings of the National Academy of Sciences of the United States of America·Ilya BelevichMichael I Verkhovsky
Jun 10, 2016·Scientific Reports·Sinan Al-AttarSimon de Vries
Jan 6, 2021·Chemical Reviews·Filipa CalistoManuela M Pereira
Mar 1, 2011·Biochimica Et Biophysica Acta·Vitaliy B BorisovAlessandro Giuffrè
Jul 16, 2011·Biochimica Et Biophysica Acta·Vitaliy B BorisovMichael I Verkhovsky

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