Direct measurement of proton release by cytochrome c oxidase in solution during the F-->O transition

Proceedings of the National Academy of Sciences of the United States of America
D ZaslavskyR B Gennis

Abstract

The mechanism by which electron transfer is coupled to proton pumping in cytochrome c oxidase is a major unsolved problem in molecular bioenergetics. In this work it is shown that, at least under some conditions, proton release from the enzyme occurs before proton uptake upon electron transfer to the heme/Cu active site of the enzyme. This sequence is similar to that of proton release and uptake observed for the light-activated proton pump bacteriorhodopsin. In the case of cytochrome c oxidase, this observation means that both the ejected proton and the proton required for the chemistry at the enzyme active site must come from an internal proton pool.

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Citations

Jun 9, 2006·Photochemical & Photobiological Sciences : Official Journal of the European Photochemistry Association and the European Society for Photobiology·Armen Y Mulkidjanian, Dmitry A Cherepanov
Jan 13, 2012·The Journal of Biological Chemistry·Kristina KirchbergUlrike Alexiev
Jun 8, 2006·Annual Review of Biochemistry·Jonathan P HoslerDenise A Mills
Jan 13, 2006·Proceedings of the National Academy of Sciences of the United States of America·Gisela BrändénPeter Brzezinski
Nov 25, 2005·Proceedings of the National Academy of Sciences of the United States of America·Lina SalomonssonPeter Brzezinski
Apr 21, 2006·Biochimica Et Biophysica Acta·Armen Y MulkidjanianDmitry A Cherepanov
Jun 20, 2006·Biochimica Et Biophysica Acta·Armen Y Mulkidjanian
Jul 11, 2006·Biochimica Et Biophysica Acta·Gisela BrändénPeter Brzezinski
Oct 19, 2019·Journal of Molecular Biology·Giuseppe CapitanioSergio Papa
Jan 21, 2015·Chemical Reviews·Shinya Yoshikawa, Atsuhiro Shimada

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