| Autor: |
Zhang Y; School of Chemical Sciences, University of Illinois at Urbana─Champaign, Urbana, Illinois 61801, United States., Tao L; Department of Chemistry, University of California, Davis, California 95616, United States., Woods TJ; School of Chemical Sciences, University of Illinois at Urbana─Champaign, Urbana, Illinois 61801, United States., Britt RD; Department of Chemistry, University of California, Davis, California 95616, United States., Rauchfuss TB; School of Chemical Sciences, University of Illinois at Urbana─Champaign, Urbana, Illinois 61801, United States. |
| Abstrakt: |
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 H 2 . 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 [Fe 2 (μ-SH) 2 (CN) 2 (CO) 4 ] 2- active HydA1 can be biosynthesized without maturases HydG and HydE. |
