Please use this identifier to cite or link to this item: http://dx.doi.org/10.25673/119485
Title: Biosynthesis and assembly of hydrogenase [NiFe]-cofactor : recent advances and perspectives
Author(s): Sawers, R. Gary
Hardelt, Maximilian
Haase, AlexanderLook up in the Integrated Authority File of the German National Library
Lubek, Dorothea
Issue Date: 2025
Type: Article
Language: English
Abstract: The large subunit of all [NiFe]-hydrogenases in bacteria and archaea has a heterobimetallic NiFe(CN)2CO cofactor coordinated by four cysteine residues. The iron ion has two cyanides and a carbon monoxide as diatomic ligands. Six ancillary Hyp (ABCDEF) proteins are necessary for anaerobic synthesis of this cofactor, while under oxic conditions at least one further protein, HypX, is required for CO synthesis. The Fe(CN)2CO moiety of the cofactor is synthesized on a separate HypCD scaffold complex. Nickel is inserted into the apo-large subunit only after Fe(CN)2CO has been introduced. Recent biochemical and structural studies have significantly advanced our understanding of cofactor biosynthesis for these important metalloenzymes. Despite these gains in mechanistic insight, many questions still remain, the most pressing of which is the origin of the CO ligand in anaerobic microorganisms. This minireview provides an overview of the current status of this research field and highlights recent advances and unresolved issues.
URI: https://opendata.uni-halle.de//handle/1981185920/121443
http://dx.doi.org/10.25673/119485
Open Access: Open access publication
License: (CC BY 4.0) Creative Commons Attribution 4.0(CC BY 4.0) Creative Commons Attribution 4.0
Journal Title: Metallomics
Publisher: [Verlag nicht ermittelbar]
Publisher Place: Oxford University Press
Volume: 17
Issue: 6
Original Publication: 10.1093/mtomcs/mfaf015
Appears in Collections:Open Access Publikationen der MLU

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