The timing of proton migration in membrane-reconstituted cytochrome c oxidase

Autor: Lina Salomonsson, Peter Brzezinski, Pia Ädelroth, Kristina Faxén
Rok vydání: 2005
Předmět:
Zdroj: Proceedings of the National Academy of Sciences. 102:17624-17629
ISSN: 1091-6490
0027-8424
DOI: 10.1073/pnas.0505431102
Popis: In mitochondria and aerobic bacteria energy conservation involves electron transfer through a number of membrane-bound protein complexes to O 2 . The reduction of O 2 , accompanied by the uptake of substrate protons to form H 2 O, is catalyzed by cytochrome c oxidase (C c O). This reaction is coupled to proton translocation (pumping) across the membrane such that each electron transfer to the catalytic site is linked to the uptake of two protons from one side and the release of one proton to the other side of the membrane. To address the mechanism of vectorial proton translocation, in this study we have investigated the solvent deuterium isotope effect of proton-transfer rates in C c O oriented in small unilamellar vesicles. Although in H 2 O the uptake and release reactions occur with the same rates, in D 2 O the substrate and pumped protons are taken up first (τ D ≅ 200 μs, “peroxy” to “ferryl” transition) followed by a significantly slower proton release to the other side of the membrane (τ D ≅ 1 ms). Thus, the results define the order and timing of the proton transfers during a pumping cycle. Furthermore, the results indicate that during C c O turnover internal electron transfer to the catalytic site is controlled by the release of the pumped proton, which suggests a mechanism by which C c O orchestrates a tight coupling between electron transfer and proton translocation.
Databáze: OpenAIRE