Premium
The Di‐Iron Subsite of All‐Iron Hydrogenase: Mechanism of Cyanation of a Synthetic {2Fe3S}–Carbonyl Assembly
Author(s) -
George Simon J.,
Cui Zhen,
Razavet Mathieu,
Pickett Christopher J.
Publication year - 2002
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/1521-3765(20020902)8:17<4037::aid-chem4037>3.0.co;2-o
Subject(s) - cyanation , chemistry , hydrogenase , kinetics , bridging (networking) , combinatorial chemistry , mechanism (biology) , stereochemistry , catalysis , biochemistry , computer network , physics , quantum mechanics , computer science , philosophy , epistemology
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.