Organometallic Fe <sub>2</sub> (μ-SH) <sub>2</sub> (CO) <sub>4</sub> (CN) <sub>2</sub> Cluster 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
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.
Topics & Concepts
ChemistryHydrogenaseBiosynthesisCluster (spacecraft)CatalysisAdductActive siteSubstrate (aquarium)EnzymeStereochemistryOrganic chemistryProgramming languageGeologyOceanographyComputer scienceMetalloenzymes and iron-sulfur proteinsElectrocatalysts for Energy ConversionAdvanced battery technologies research