Related Experiment Video
Updated: Jun 13, 2025

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
Published on: July 20, 2022
Structural and functional mechanisms of cytochrome c oxidase
Denis L Rousseau1, Izumi Ishigami1, Syun-Ru Yeh1
1Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
None:
Cytochrome c oxidase (CcO) is the terminal enzyme in the electron transfer chain in mitochondria. It catalyzes the four-electron reduction of O2 to H2O and harnesses the redox energy to drive unidirectional proton translocation against a proton electrochemical gradient. A great deal of research has been conducted to comprehend the molecular properties of CcO. However, the mechanism by which the oxygen reduction reaction is coupled to proton translocation remains poorly understood. Here, we review the chemical properties of a variety of key oxygen intermediates of bovine CcO (bCcO) revealed by time-resolved resonance Raman spectroscopy and the structural features of the enzyme uncovered by serial femtosecond crystallography, an innovative technique that allows structural determination at room temperature without radiation damage. The implications of these data on the proton translocation mechanism are discussed.
Related Concept Videos
Electron Transport Chain: Complex III and IV
The Supercomplexes in the Crista Membrane
Electron Transport Chain: Complex I and II
ROS generation is regulated and maintained at moderate levels necessary...
ATP Synthase: Mechanism
Introduction to Mechanisms of Enzyme Catalysis
Electron Transport Chains
The ETC is comprised of...

