Organometallic Fe2(μ-SH)2(CO)4(CN)2Cluster Allows the Biosynthesis of the [FeFe]-Hydrogenase with only the HydF Maturase

Yu Zhang; Lizhi Tao; Toby J. Woods; R. David Britt; Thomas B. Rauchfuss

doi:10.1021/jacs.1c12506

Organometallic Fe₂(μ-SH)₂(CO)₄(CN)₂Cluster Allows the Biosynthesis of the [FeFe]-Hydrogenase with only the HydF Maturase

Yu Zhang, Lizhi Tao, Toby J. Woods, R. David Britt, Thomas B. Rauchfuss

Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

The biosynthesis of the active site of the [FeFe]-hydrogenases (HydA1), the H-cluster, is of interest because these enzymes are highly efficient catalysts for the oxidation and production of H2. The biosynthesis of the [2Fe]H subcluster of the H-cluster proceeds from simple precursors, which are processed by three maturases: HydG, HydE, and HydF. Previous studies established that HydG produces an Fe(CO)2(CN) adduct of cysteine, which is the substrate for HydE. In this work, we show that by using the synthetic cluster [Fe2(μ-SH)2(CN)2(CO)4]2- active HydA1 can be biosynthesized without maturases HydG and HydE.

Original language	English (US)
Pages (from-to)	1534-1538
Number of pages	5
Journal	Journal of the American Chemical Society
Volume	144
Issue number	4
DOIs	https://doi.org/10.1021/jacs.1c12506
State	Published - Feb 2 2022

ASJC Scopus subject areas

General Chemistry
Biochemistry
Catalysis
Colloid and Surface Chemistry

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10.1021/jacs.1c12506

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title = "Organometallic Fe2(μ-SH)2(CO)4(CN)2Cluster Allows the Biosynthesis of the [FeFe]-Hydrogenase with only the HydF Maturase",

abstract = "The biosynthesis of the active site of the [FeFe]-hydrogenases (HydA1), the H-cluster, is of interest because these enzymes are highly efficient catalysts for the oxidation and production of H2. The biosynthesis of the [2Fe]H subcluster of the H-cluster proceeds from simple precursors, which are processed by three maturases: HydG, HydE, and HydF. Previous studies established that HydG produces an Fe(CO)2(CN) adduct of cysteine, which is the substrate for HydE. In this work, we show that by using the synthetic cluster [Fe2(μ-SH)2(CN)2(CO)4]2- active HydA1 can be biosynthesized without maturases HydG and HydE.",

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AU - Woods, Toby J.

AU - Britt, R. David

AU - Rauchfuss, Thomas B.

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