Issue 15, 2024

Outer-sphere effects on the O2 sensitivity, catalytic bias and catalytic reversibility of hydrogenases

Abstract

The comparison of homologous metalloenzymes, in which the same inorganic active site is surrounded by a variable protein matrix, has demonstrated that residues that are remote from the active site may have a great influence on catalytic properties. In this review, we summarise recent findings on the diverse molecular mechanisms by which the protein matrix may define the oxygen tolerance, catalytic directionality and catalytic reversibility of hydrogenases, enzymes that catalyse the oxidation and evolution of H2. These mechanisms involve residues in the second coordination sphere of the active site metal ion, more distant residues affecting protein flexibility through their side chains, residues lining the gas channel and even accessory subunits. Such long-distance effects, which contribute to making enzymes efficient, robust and different from one another, are a source of wonder for biochemists and a challenge for synthetic bioinorganic chemists.

Graphical abstract: Outer-sphere effects on the O2 sensitivity, catalytic bias and catalytic reversibility of hydrogenases

Supplementary files

Article information

Article type
Perspective
Submitted
29 jan. 2024
Accepted
15 mar. 2024
First published
15 mar. 2024
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY-NC license

Chem. Sci., 2024,15, 5418-5433

Outer-sphere effects on the O2 sensitivity, catalytic bias and catalytic reversibility of hydrogenases

A. Fasano, V. Fourmond and C. Léger, Chem. Sci., 2024, 15, 5418 DOI: 10.1039/D4SC00691G

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