Formate hydrogenlyase: A group 4 [NiFe]-hydrogenase in tandem with a formate dehydrogenase.

Autor:	Finney AJ; Devonshire Centre for Biosystems Science & Engineering, School of Natural & Environmental Sciences, Newcastle University, Newcastle-Upon-Tyne NE1 7RU, England, United Kingdom., Sargent F; Devonshire Centre for Biosystems Science & Engineering, School of Natural & Environmental Sciences, Newcastle University, Newcastle-Upon-Tyne NE1 7RU, England, United Kingdom.
Jazyk:	angličtina
Zdroj:	Advances in microbial physiology [Adv Microb Physiol] 2019; Vol. 74, pp. 465-486. Date of Electronic Publication: 2019 Feb 28.
DOI:	10.1016/bs.ampbs.2019.02.004
Abstrakt:	Hydrogenase enzymes are currently under the international research spotlight due to emphasis on biologically produced hydrogen as one potential energy carrier to relinquish the requirement for 'fossil fuel' derived energy. Three major classes of hydrogenase exist in microbes all able to catalyze the reversible oxidation of dihydrogen to protons and electrons. These classes are defined by their active site metal content: [NiFe]-; [FeFe]- and [Fe]-hydrogenases. Of these the [NiFe]-hydrogenases have links to ancient forms of metabolism, utilizing hydrogen as the original source of reductant on Earth. This review progresses to highlight the Group 4 [NiFe]-hydrogenase enzymes that preferentially generate hydrogen exploiting various partner enzymes or ferredoxin, while in some cases translocating ions across biological membranes. Specific focus is paid to Group 4A, the Formate hydrogenlyase complexes. These are the combination of a six or nine subunit [NiFe]-hydrogenase with a soluble formate dehydrogenase to derived electrons from formate oxidation for proton reduction. The incidence, physiology, structure and biotechnological application of these complexes will be explored with attention on Escherichia coli Formate Hydrogenlyase-1 (FHL-1). (Copyright © 2019 Elsevier Ltd. All rights reserved.)
Databáze:	MEDLINE
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