A personal account on 25 years of scientific literature on [FeFe]-hydrogenase.

Autor: Sidabras JW; Department of Biophysics, Medical College of Wisconsin, 8701 Watertown Plank Rd, Milwaukee, WI, USA, 53226. jwsidabras@mcw.edu., Stripp ST; Department of Physics, Freie Universität Berlin, Arnimallee 14, 14195, Berlin, Germany. sven.stripp@gmail.com.
Jazyk: angličtina
Zdroj: Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry [J Biol Inorg Chem] 2023 Jun; Vol. 28 (4), pp. 355-378. Date of Electronic Publication: 2023 Mar 01.
DOI: 10.1007/s00775-023-01992-5
Abstrakt: [FeFe]-hydrogenases are gas-processing metalloenzymes that catalyze H 2 oxidation and proton reduction (H 2 release) in microorganisms. Their high turnover frequencies and lack of electrical overpotential in the hydrogen conversion reaction has inspired generations of biologists, chemists, and physicists to explore the inner workings of [FeFe]-hydrogenase. Here, we revisit 25 years of scientific literature on [FeFe]-hydrogenase and propose a personal account on 'must-read' research papers and review article that will allow interested scientists to follow the recent discussions on catalytic mechanism, O 2 sensitivity, and the in vivo synthesis of the active site cofactor with its biologically uncommon ligands carbon monoxide and cyanide. Focused on-but not restricted to-structural biology and molecular biophysics, we highlight future directions that may inspire young investigators to pursue a career in the exciting and competitive field of [FeFe]-hydrogenase research.
(© 2023. The Author(s), under exclusive licence to Society for Biological Inorganic Chemistry (SBIC).)
Databáze: MEDLINE
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