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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Monophosphate / metabolism
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Adenosine Triphosphate / metabolism
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Amino Acid Motifs
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Bacterial Proteins / chemistry
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Bacterial Proteins / metabolism*
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Carbamyl Phosphate / metabolism
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Carbon Monoxide / metabolism
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Catalysis
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Cyanides / chemistry
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Cyanides / metabolism*
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Cysteine / chemistry
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Cysteine / metabolism
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Escherichia coli Proteins / metabolism
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Hydrogenase / chemistry
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Hydrogenase / metabolism*
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Iron / chemistry
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Iron / metabolism*
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Ligands
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Mass Spectrometry
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Models, Chemical
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Oxidation-Reduction
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Thiocyanates / metabolism*
Substances
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Bacterial Proteins
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Cyanides
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Escherichia coli Proteins
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HypF protein, Bacteria
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Ligands
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Thiocyanates
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hypE protein, Bacteria
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Adenosine Monophosphate
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Carbamyl Phosphate
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Carbon Monoxide
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Adenosine Triphosphate
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thiocyanic acid
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Iron
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nickel-iron hydrogenase
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Hydrogenase
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Cysteine