Review
Copyright ©The Author(s) 2020. Published by Baishideng Publishing Group Inc. All rights reserved.
World J Biol Chem. Sep 27, 2020; 11(2): 52-61
Published online Sep 27, 2020. doi: 10.4331/wjbc.v11.i2.52
Regulation of cytochrome c oxidase contributes to health and optimal life
Bernhard Kadenbach
Bernhard Kadenbach, Department of Chemistry/Biochemistry, Fachbereich Chemie, Philipps-Universität Marburg, Marburg D-35043, Hessen, Germany
Author contributions: Kadenbach B solely contributed to this manuscript.
Conflict-of-interest statement: No conflict of interests.
Open-Access: This article is an open-access article that was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution NonCommercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: http://creativecommons.org/licenses/by-nc/4.0/
Corresponding author: Bernhard Kadenbach, DSc, PhD, Emeritus Professor, Department of Chemistry/Biochemistry, Fachbereich Chemie, Philipps-Universität Marburg, Marburg D-35043, Hessen, Germany. kadenbach@staff.uni-marburg.de
Received: April 16, 2020
Peer-review started: April 16, 2020
First decision: July 25, 2020
Revised: August 1, 2020
Accepted: August 24, 2020
Article in press: August 24, 2020
Published online: September 27, 2020
Processing time: 160 Days and 19.4 Hours
Core Tip

Core Tip: This article describes the “allosteric ATP-inhibition of cytochrome c oxidase,” which prevents the formation of reactive oxygen species (ROS) under resting conditions in all eukaryotic cells by keeping the mitochondrial membrane potential ΔΨm at low values. Under stress – via increased calcium concentrations – this mechanism is switched off, accompanied by increased rates of ATP-synthesis with decreased efficiency and formation of deleterious ROS. A hypothesis is described in which NDUFA4 changes its position from complex I to cytochrome c oxidase when the metabolic state changes from the rest to excited state under stress.