The di-iron subsite of all-iron hydrogenase: mechanism of cyanation of a synthetic [2Fe3S]-carbonyl assembly.
This paper describes the kinetics and intimate mechanisms associated with cyanation of [2Fe3S] assemblies to give species structurally related to the subsite of all-iron hydrogenase. Stopped-flow FTIR spectroscopy has enabled the quantitation of the dynamics of five well-defined steps that experimentally illustrate the role of bridging carbonyls in the assembly of the dicyanide species, how on-off sulfur ligation can have a dramatic effect on cyanation kinetics and how the [2Fe3S] core stabilises bridging carbonyl species.
D002248:Carbon Monoxide / Q000737:chemistry; D003486:Cyanides / Q000737:chemistry*; D006864:Hydrogenase / Q000737:chemistry* / Q000378:metabolism; D008024:Ligands; D015394:Molecular Structure; D017550:Spectroscopy, Fourier Transform Infrared; D013440:Sulfides / Q000737:chemistry
D003486:Cyanides; D008024:Ligands; D013440:Sulfides; D002248:Carbon Monoxide; D006864:Hydrogenase