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Metallocofactor assembly for [FeFe]-hydrogenases

Metallocofactor assembly for [FeFe]-hydrogenases
Metallocofactor assembly for [FeFe]-hydrogenases
Hydrogenases are a potential source of environmentally benign bioenergy, using complex cofactors to catalyze the reversible reduction of protons to form hydrogen. The most active subclass, the [FeFe]-hydrogenases, is dependent on a metallocofactor, the H cluster, that consists of a two iron subcluster ([2Fe]H) bridging to a classical cubane cluster ([4Fe–4S]H). The ligands coordinating to the diiron subcluster include an azadithiolate, three carbon monoxides, and two cyanides. To assemble this complex cofactor, three maturase enzymes, HydG, HydE and HydF are required. The biosynthesis of the diatomic ligands proceeds by an unusual fragmentation mechanism, and structural studies in combination with spectroscopic analysis have started to provide insights into the HydG mediated assembly of a [2Fe]H subcluster precursor.
0959-440X
90-97
Dinis, Pedro
40a6c6d3-c9f3-44fc-809b-c865d203ce74
Wieckowski, Beata
a8ab31d2-68c4-41c8-b666-8edbe3a805e4
Roach, Peter
ca94060c-4443-482b-af3e-979243488ba9
Dinis, Pedro
40a6c6d3-c9f3-44fc-809b-c865d203ce74
Wieckowski, Beata
a8ab31d2-68c4-41c8-b666-8edbe3a805e4
Roach, Peter
ca94060c-4443-482b-af3e-979243488ba9

Dinis, Pedro, Wieckowski, Beata and Roach, Peter (2016) Metallocofactor assembly for [FeFe]-hydrogenases. Current Opinion in Structural Biology, 41, 90-97. (doi:10.1016/j.sbi.2016.06.004).

Record type: Article

Abstract

Hydrogenases are a potential source of environmentally benign bioenergy, using complex cofactors to catalyze the reversible reduction of protons to form hydrogen. The most active subclass, the [FeFe]-hydrogenases, is dependent on a metallocofactor, the H cluster, that consists of a two iron subcluster ([2Fe]H) bridging to a classical cubane cluster ([4Fe–4S]H). The ligands coordinating to the diiron subcluster include an azadithiolate, three carbon monoxides, and two cyanides. To assemble this complex cofactor, three maturase enzymes, HydG, HydE and HydF are required. The biosynthesis of the diatomic ligands proceeds by an unusual fragmentation mechanism, and structural studies in combination with spectroscopic analysis have started to provide insights into the HydG mediated assembly of a [2Fe]H subcluster precursor.

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Dinis Metallocofactor Assembly CoStBi 2016 v1.pdf - Accepted Manuscript
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Accepted/In Press date: 23 June 2016
e-pub ahead of print date: 23 June 2016
Published date: December 2016

Identifiers

Local EPrints ID: 397330
URI: http://eprints.soton.ac.uk/id/eprint/397330
ISSN: 0959-440X
PURE UUID: c3c31ae0-8c00-4dcf-8ce3-7eaeed754b25
ORCID for Peter Roach: ORCID iD orcid.org/0000-0001-9880-2877

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Date deposited: 24 Jun 2016 13:43
Last modified: 07 Oct 2020 04:54

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