1. Final Stages in the Biosynthesis of the [FeFe]-Hydrogenase Active Site.
- Author
-
Yu X, Rao G, Britt RD, and Rauchfuss TB
- Subjects
- Molecular Structure, Hydrogenase metabolism, Hydrogenase chemistry, Catalytic Domain, Iron-Sulfur Proteins chemistry, Iron-Sulfur Proteins metabolism
- Abstract
The paper aims to elucidate the final stages in the biosynthesis of the [2Fe]
H active site of the [FeFe]-hydrogenases. The recently hypothesized intermediate [Fe2 (SCH2 NH2 )2 (CN)2 (CO)4 ]2- ([1]2- ) was prepared by a multistep route from [Fe2 (S2 )(CN)(CO)5 ]- . The following synthetic intermediates were characterized in order: [Fe2 (SCH2 NHFmoc)2 (CNBEt3 )(CO)5 ]- , [Fe2 (SCH2 NHFmoc)2 (CN)-(CO)5 ]- , and [Fe2 (SCH2 NHFmoc)2 (CN)2 (CO)4 ]2- , where Fmoc is fluorenylmethoxycarbonyl). Derivatives of these anions include [K(18-crown-6)]+ , PPh4 + and PPN+ salts as well as the13 CD2 -isotopologues. These Fe2 species exist as a mixture of two isomers attributed to diequatorial (ee) and axial-equatorial (ae) stereochemistry at sulfur. In vitro experiments demonstrate that [1]2- maturates HydA1 in the presence of HydF and a cocktail of reagents. HydA1 can also be maturated using a highly simplified cocktail, omitting HydF and other proteins. This result is consistent with HydA1 participating in the maturation process and refines the roles of HydF., (© 2024 The Authors. Angewandte Chemie International Edition published by Wiley-VCH GmbH.)- Published
- 2024
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