NDLI: The catalytic cycle of cytochrome c oxidase is not the sum of its two halves

Content Provider	PubMed Central
Author	Bloch, Dmitry Ilya, Belevich Jasaitis, Audrius Ribacka, Camilla Puustinen, Anne Verkhovsky, Michael I. Wikström, Mårten
Copyright Year	2004
Abstract	Membrane-bound cytochrome c oxidase catalyzes cell respiration in aerobic organisms and is a primary energy transducer in biology. The two halves of the catalytic cycle may be studied separately: in an oxidative phase, the enzyme is oxidized by O2, and in a reductive phase, the oxidized enzyme is reduced before binding the next O2 molecule. Here we show by time-resolved membrane potential and pH measurements with cytochrome oxidase liposomes that, with both phases in succession, two protons are translocated during each phase, one during each individual electron transfer step. However, when the reductive phase is not immediately preceded by oxidation, it follows a different reaction pathway no longer coupled to proton pumping. Metastable states with altered redox properties of the metal centers are accessed during turnover and relax when external electron donors are exhausted but recover after enzyme reduction and reoxidation by O2. The efficiency of ATP synthesis might be regulated by switching between the two catalytic pathways.
Related Links	http://dx.doi.org/10.1073/pnas.0306036101
Ending Page	533
Page Count	5
Starting Page	529
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	2
Volume Number	101
Language	English
Publisher	National Academy of Sciences
Publisher Date	2004-01-13
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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The catalytic cycle of cytochrome c oxidase is not the sum of its two halves

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