Taming of a Poison: Biosynthesis of the NiFe-Hydrogenase Cyanide Ligands

@article{Reissmann2003TamingOA,
  title={Taming of a Poison: Biosynthesis of the NiFe-Hydrogenase Cyanide Ligands},
  author={S. Reissmann and E. Hochleitner and Haofan Wang and A. Paschos and F. Lottspeich and R. Glass and A. B{\"o}ck},
  journal={Science},
  year={2003},
  volume={299},
  pages={1067 - 1070}
}
NiFe-hydrogenases have an Ni-Fe site in which the iron has one CO and two CN groups as ligands. Synthesis of the CN ligands requires the activity of two hydrogenase maturation proteins: HypF and HypE. HypF is a carbamoyltransferase that transfers the carbamoyl moiety of carbamoyladenylate to the COOH-terminal cysteine of HypE and thus forms an enzyme-thiocarbamate. HypE dehydrates theS-carbamoyl moiety in an adenosine triphosphate–dependent process to yield the enzyme thiocyanate. Chemical… Expand
[NiFe]‐Hydrogenase Cofactor Assembly
Heterodimeric [NiFe]-hydrogenases catalyze the activation of dihydrogen. The large subunit of all [NiFe]-hydrogenases studied to date harbors a bimetallic catalytic center comprising a nickel ion andExpand
Crystal structures of the carbamoylated and cyanated forms of HypE for [NiFe] hydrogenase maturation
TLDR
These structures reveal the detailed interactions around the carbamoylated and cyanated cysteine, providing structural basis for the biological conversion of primary amide to nitrile, and suggest that Lys134 functions as a proton acceptor in the dehydration of thiocarboxamide. Expand
Carbamoylphosphate serves as the source of CN−, but not of the intrinsic CO in the active site of the regulatory [NiFe]‐hydrogenase from Ralstonia eutropha
TLDR
Infrared spectroscopy of purified hydrogenase provided direct evidence that only the cyanide ligands, but not the CO ligand, originate from CO2 and carbamoylphosphate, and incorporation of label from 13CO exclusively into the carbonyl ligand indicates that free CO is a possible precursor in carbonyL ligand biosynthesis. Expand
The Influence of Oxygen on [NiFe]–Hydrogenase Cofactor Biosynthesis and How Ligation of Carbon Monoxide Precedes Cyanation
TLDR
An FT–IR spectroscopic analysis of HypC–HypD isolated from a hydrogenase–competent wild–type strain of Escherichia coli suggests that CO ligation precedes cyanation in vivo, and provides a rationale for the deleterious effects of O2 on in vivo cofactor biosynthesis. Expand
Identification of an Isothiocyanate on the HypEF Complex Suggests a Route for Efficient Cyanyl–Group Channeling during [NiFe]–Hydrogenase Cofactor Generation
TLDR
The IR signature of HypE could ultimately be assigned to isothiocyanate (–N=C=S) rather than thiOCyanate(–S–C≡N), which has important implications for cyanyl–group channeling during [NiFe]–hydrogenase cofactor generation. Expand
The complex between hydrogenase-maturation proteins HypC and HypD is an intermediate in the supply of cyanide to the active site iron of [NiFe]-hydrogenases.
TLDR
The results suggest the existence of a dynamic complex between the hydrogenase maturation proteins HypD, HypC, HypE and HypF, which is the site of ligand biosynthesis and attachment to the iron atom of the NiFe site in hydrogenase 3. Expand
Probing the Origin of the Metabolic Precursor of the CO Ligand in the Catalytic Center of [NiFe] Hydrogenase*
TLDR
The results indicate at least two different pathways for biosynthesis of the CO ligand of [NiFe] hydrogenase, and the data indicate multiple, growth mode-dependent biosynthetic pathways for the carbonyl ligand. Expand
[NiFe]-Hydrogenase Maturation.
TLDR
Recent work illuminating how the accessory proteins contribute to the maturation of [NiFe]-hydrogenase is reviewed and some of the outstanding questions that remain to be resolved are discussed. Expand
The importance of iron in the biosynthesis and assembly of [NiFe]-hydrogenases
TLDR
Genetic analyses have provided evidence for the existence of key checkpoints during cofactor biosynthesis and enzyme assembly that ensure correct spatiotemporal maturation of these modular oxidoreductases. Expand
[NiFe]‐hydrogenase maturation: Isolation of a HypC–HypD complex carrying diatomic CO and CN− ligands
TLDR
Using infrared spectroscopy, it is demonstrated that an anaerobically purified, Strep‐tagged HypCD complex from Escherichia coli exhibits absorption bands characteristic of diatomic CO and CN− ligands as well as CO2, suggesting that the HypCDcomplex carries minimally the Fe(CN)2CO cofactor. Expand
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