Redox Activity of Cytochromes from the Respiratory Chain

Melin, Frédéric; Nikolaev, Anton; Hellwig, Petra

doi:10.1016/b978-0-12-409547-2.13899-5

Cited by 1 publication

(1 citation statement)

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“…The redox potentials of hemes span up to 0.8 V, and in the respiratory chains, values from −150 to +500 mV have been reported. , The redox potential depends on various factors, ,,,− including the nature of the axial ligands, the electrostatic interactions between the metal and the propionate side chains, − as well as the hydrophobicity/water accessibility of the heme binding pocket . External factors, such as pH and ionic strength, may also influence the redox properties of hemes.…”

Section: Introductionmentioning

confidence: 99%

Redox Properties of the Membrane Proteins from the Respiratory Chain

Melin

Hellwig

2020

Chem. Rev.

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This review focuses on the electrochemical and spectroelectrochemical studies that gave insight into redox potentials of the four mitochondrial complexes and their homologues from bacterial respiratory chains using O2 as a terminal acceptor, thus providing crucial information about their reaction mechanism. Advantages and limitations of the use of the different techniques for the study of membrane proteins are presented. Electrocatalytic experiments are described that revealed specific features of the reaction with the substrates and inhibitors. An overview is given on the great variability of the redox and catalytic properties of the enzymes in different organisms that may be due to adaptation to the specific environments in which these enzymes function. The adaptation of the redox chain to the different types of quinone and substrates is analyzed, and future studies are discussed.

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