Unknown

Dataset Information

0

Mechanistic insight into the nitrosylation of the [4Fe-4S] cluster of WhiB-like proteins.


ABSTRACT: The reactivity of protein bound iron-sulfur clusters with nitric oxide (NO) is well documented, but little is known about the actual mechanism of cluster nitrosylation. Here, we report studies of members of the Wbl family of [4Fe-4S] containing proteins, which play key roles in regulating developmental processes in actinomycetes, including Streptomyces and Mycobacteria, and have been shown to be NO responsive. Streptomyces coelicolor WhiD and Mycobacterium tuberculosis WhiB1 react extremely rapidly with NO in a multiphasic reaction involving, remarkably, 8 NO molecules per [4Fe-4S] cluster. The reaction is 10(4)-fold faster than that observed with O(2) and is by far the most rapid iron-sulfur cluster nitrosylation reaction reported to date. An overall stoichiometry of [Fe(4)S(4)(Cys)(4)](2-) + 8NO ? 2[Fe(I)(2)(NO)(4)(Cys)(2)](0) + S(2-) + 3S(0) has been established by determination of the sulfur products and their oxidation states. Kinetic analysis leads to a four-step mechanism that accounts for the observed NO dependence. DFT calculations suggest the possibility that the nitrosylation product is a novel cluster [Fe(I)(4)(NO)(8)(Cys)(4)](0) derived by dimerization of a pair of Roussin's red ester (RRE) complexes.

SUBMITTER: Crack JC 

PROVIDER: S-EPMC3117330 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

Mechanistic insight into the nitrosylation of the [4Fe-4S] cluster of WhiB-like proteins.

Crack Jason C JC   Smith Laura J LJ   Stapleton Melanie R MR   Peck Jamie J   Watmough Nicholas J NJ   Buttner Mark J MJ   Buxton Roger S RS   Green Jeffrey J   Oganesyan Vasily S VS   Thomson Andrew J AJ   Le Brun Nick E NE  

Journal of the American Chemical Society 20101223 4


The reactivity of protein bound iron-sulfur clusters with nitric oxide (NO) is well documented, but little is known about the actual mechanism of cluster nitrosylation. Here, we report studies of members of the Wbl family of [4Fe-4S] containing proteins, which play key roles in regulating developmental processes in actinomycetes, including Streptomyces and Mycobacteria, and have been shown to be NO responsive. Streptomyces coelicolor WhiD and Mycobacterium tuberculosis WhiB1 react extremely rapi  ...[more]

Similar Datasets

2021-08-16 | E-MTAB-10818 | biostudies-arrayexpress
| S-EPMC5204455 | biostudies-literature
| S-EPMC7939391 | biostudies-literature
| S-EPMC2785490 | biostudies-literature
| S-EPMC3807426 | biostudies-literature
| S-EPMC3819817 | biostudies-literature
| S-EPMC3570669 | biostudies-literature
| S-EPMC3107574 | biostudies-literature
| S-EPMC2805927 | biostudies-literature
| S-EPMC21691 | biostudies-literature