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Updated: May 30, 2026

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
Published on: March 18, 2012
The origin of the Fe(IV)=O intermediates in cytochrome aa(3) oxidase
Eftychia Pinakoulaki1, Vangelis Daskalakis, Constantinos Varotsis
1Department of Chemistry, University of Cyprus, Nicosia, Cyprus.
Abstract:
The dioxygen reduction mechanism in cytochrome oxidases relies on proton control of the electron transfer events that drive the process. Proton delivery and proton channels in the protein that are relevant to substrate reduction and proton pumping are considered, and the current status of this area is summarized. We propose a mechanism in which the coupling of the oxygen reduction chemistry to proton translocation (P→F transition) is related to the properties of two groups of highly conserved residues, namely, His411/G386-T389 and the heme a(3)-propionateA-D399-H403 chain.
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