Litcius/Paper detail

Final Stages in the Biosynthesis of the [FeFe]‐Hydrogenase Active Site

Xin Yu, Guodong Rao, R. David Britt, Thomas B. Rauchfuss

2024Angewandte Chemie International Edition11 citationsDOIOpen Access PDF

Abstract

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 [Fe 2 (SCH 2 NH 2 ) 2 (CN) 2 (CO) 4 ] 2− ([ 1 ] 2− ) was prepared by a multistep route from [Fe 2 (S 2 )(CN)(CO) 5 ] − . The following synthetic intermediates were characterized in order: [Fe 2 (SCH 2 NHFmoc) 2 (CNBEt 3 )(CO) 5 ] − , [Fe 2 (SCH 2 NHFmoc) 2 (CN)−(CO) 5 ] − , and [Fe 2 (SCH 2 NHFmoc) 2 (CN) 2 (CO) 4 ] 2− , where Fmoc is fluorenylmethoxycarbonyl). Derivatives of these anions include [K(18‐crown‐6)] + , PPh 4 + and PPN + salts as well as the 13 CD 2 ‐isotopologues. These Fe 2 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.

Topics & Concepts

HydrogenaseChemistryIsotopologueBiosynthesisReagentActive siteSulfurStereochemistryCombinatorial chemistryCatalysisMedicinal chemistryMoleculeEnzymeOrganic chemistryMetalloenzymes and iron-sulfur proteinsElectrocatalysts for Energy ConversionAsymmetric Hydrogenation and Catalysis