Carbamoylphosphate requirement for synthesis of the active center of [NiFe]-hydrogenases.
The iron of the binuclear active center of [NiFe]-hydrogenases carries two CN and one CO ligands which are thought to confer to the metal a low oxidation and/or spin state essential for activity. Based on the observation that one of the seven auxiliary proteins required for the synthesis and insertion of the [NiFe] cluster contains a sequence motif characteristic of O-carbamoyl-transferases it was discovered that carbamoyl phosphate is essential for formation of active [NiFe]-hydrogenases in vivo and is specifically required for metal center synthesis suggesting that it is the source of the CO and CN ligands. A chemical path for conversion of a carbamoyl group into cyano and carbonyl moieties is postulated
Paschos
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Institute of Genetics and Microbiology, University of Munich, Germany.
Glass
R S
RS
Böck
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D020816:Amino Acid Motifs; D001665:Binding Sites; D002221:Carbamyl Phosphate / Q000378:metabolism*; D002457:Cell Extracts; D004926:Escherichia coli / Q000201:enzymology* / Q000378:metabolism; D006864:Hydrogenase / Q000096:biosynthesis* / Q000737:chemistry* / Q000378:metabolism; D007501:Iron / Q000378:metabolism*; D008024:Ligands; D008954:Models, Biological; D021122:Protein Subunits
D002457:Cell Extracts; D008024:Ligands; D021122:Protein Subunits; D002221:Carbamyl Phosphate; D007501:Iron; C043296:nickel-iron hydrogenase; D006864:Hydrogenase