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Mechanism of Oxygen Reduction in Cytochrome c Oxidase and the Role of the Active Site Tyrosine
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för organisk kemi.
2016 (engelsk)Inngår i: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 55, nr 3, s. 489-500Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Cytochrome c oxidase, the terminal enzyme in the respiratory chain, reduces molecular oxygen to water and stores the released energy through electrogenic chemistry and proton pumping across the membrane. Apart from the heme-copper binuclear center, there is a conserved tyrosine residue in the active site (BNC). The tyrosine delivers both an electron and a proton during the O-O bond cleavage step, forming a tyrosyl radical. The catalytic cycle then occurs in four reduction steps, each taking up one proton for the chemistry (water formation) and one proton to be pumped. It is here suggested that in three of the reduction steps the chemical proton enters the center of the BNC, leaving the tyrosine unprotonated with radical character. The reproprotonation of the tyrosine occurs first in the final reduction step before binding the next oxygen molecule. It is also suggested that this reduction mechanism and the presence of the tyrosine are essential for the proton pumping. Density functional theory calculations on large cluster models of the active site show that only the intermediates with the proton in the center of the BNC and with an unprotonated tyrosyl radical have a high electron affinity of similar size as the electron donor, which is essential for the ability to take up two protons per electron and thus for the proton pumping. This type of reduction mechanism is also the only one that gives a free energy profile in accordance with experimental observations for the amount of proton pumping in the working enzyme.

sted, utgiver, år, opplag, sider
2016. Vol. 55, nr 3, s. 489-500
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URN: urn:nbn:se:su:diva-127371DOI: 10.1021/acs.biochem.5b01205ISI: 000368950200008PubMedID: 26690322OAI: oai:DiVA.org:su-127371DiVA, id: diva2:910429
Tilgjengelig fra: 2016-03-09 Laget: 2016-03-02 Sist oppdatert: 2019-01-14bibliografisk kontrollert

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