Structures of the intermediates in the catalytic cycle of mitochondrial cytochrome c oxidase

2022/11/17 by Mårten Wikström, Robert B. Gennis, Peter R. Rich · 13 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · Physics and Astronomy · #ATP Synthase and ATPases Research #Biochemistry #Biology #Biophysics #Catalysis #Catalytic cycle #Chemistry #Coenzyme Q – cytochrome c reductase #Cytochrome #Cytochrome C1 #Cytochrome c #Cytochrome c oxidase #Cytosol #Electron Transport Complex IV #Electron transfer #Electron transport chain #Enzyme #Heme #Inner mitochondrial membrane #Inorganic chemistry #Membrane #Mitochondrial matrix #Mitochondrial respiratory chain #Mitochondrion #Photochemistry #Photosynthetic Processes and Mechanisms #Redox #Respiratory chain #Spectroscopy and Quantum Chemical Studies

paper · pdf · doi:10.1016/j.bbabio.2022.148933

openalex publication_date 2022/11/17 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/02

Abstract

Cytochrome c oxidase is the terminal complex of the respiratory chains in the mitochondria of nearly all eukaryotes. It catalyzes the reduction of molecular O2 to water using electrons from the respiratory chain, delivered via cytochrome c on the external surface of the inner mitochondrial membrane. The protons required for water formation are taken from the matrix side of the membrane, making catalysis vectorial. This vectorial feature is further enhanced by the fact that the redox catalysis is coupled to the translocation of protons from the inside to the outside of the inner mitochondrial membrane. We are dealing with a molecular machine that converts redox free energy into a protonmotive force (pmf). Here, we review the current extensive knowledge of the structural changes in the active heme‑copper site that accompany catalysis, based on a large variety of time-resolved spectroscopic experiments, X-ray and cryoEM structures, and advanced computational chemistry.

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