PMID:12586941
| Citation |
Reissmann, S, Hochleitner, E, Wang, H, Paschos, A, Lottspeich, F, Glass, RS and Böck, A (2003) Taming of a poison: biosynthesis of the NiFe-hydrogenase cyanide ligands. Science 299:1067-70 |
|---|---|
| Abstract |
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 the S-carbamoyl moiety in an adenosine triphosphate-dependent process to yield the enzyme thiocyanate. Chemical model reactions corroborate the feasibility of this unprecedented biosynthetic route and show that thiocyanates can donate CN to iron. This finding underscores a striking parallel between biochemistry and organometallic chemistry in the formation of an iron-cyano complex. |
| Links |
PubMed Online version:10.1126/science.1080972 |
| Keywords |
Adenosine Monophosphate/metabolism; Adenosine Triphosphate/metabolism; Amino Acid Motifs; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Carbamyl Phosphate/metabolism; Carbon Monoxide/metabolism; Catalysis; Cyanides/chemistry; Cyanides/metabolism; Cysteine/chemistry; Cysteine/metabolism; Escherichia coli Proteins/metabolism; Hydrogenase/chemistry; Hydrogenase/metabolism; Iron/chemistry; Iron/metabolism; Ligands; Mass Spectrometry; Models, Chemical; Oxidation-Reduction; Thiocyanates/metabolism |
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