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

Crack, Jason C., Smith, Laura J., Stapleton, Melanie R., Peck, Jamie, Watmough, Nicholas J., Buttner, Mark J., Buxton, Roger S., Green, Jeffrey, Oganesyan, Vasily S. ORCID: https://orcid.org/0000-0002-8738-1146, Thomson, Andrew J. and Le Brun, Nick E. ORCID: https://orcid.org/0000-0001-9780-4061 (2011) Mechanistic insight into the nitrosylation of the [4Fe−4S] cluster of WhiB-like proteins. Journal of the American Chemical Society, 133 (4). pp. 1112-1121. ISSN 0002-7863

Full text not available from this repository. (Request a copy)

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 104-fold faster than that observed with O2 and is by far the most rapid iron-sulfur cluster nitrosylation reaction reported to date. An overall stoichiometry of [Fe4S4(Cys)4]2- + 8NO ? 2[FeI2(NO)4(Cys)2]0 + S2- + 3S0 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 [FeI4(NO)8(Cys)4]0 derived by dimerization of a pair of Roussin’s red ester (RRE) complexes.

Item Type:	Article
Uncontrolled Keywords:	sdg 3 - good health and well-being ,/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_being
Faculty \ School:	Faculty of Science > School of Chemistry (former - to 2024) Faculty of Science > School of Biological Sciences
UEA Research Groups:	Faculty of Science > Research Groups > Molecular Microbiology Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017) Faculty of Science > Research Groups > Centre for Ocean and Atmospheric Sciences Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry Faculty of Science > Research Groups > Chemistry of Light and Energy Faculty of Science > Research Groups > Chemistry of Life Processes Faculty of Science > Research Groups > Centre for Photonics and Quantum Science
Depositing User:	Users 2731 not found.
Date Deposited:	14 Feb 2011 13:39
Last Modified:	24 Sep 2024 09:02
URI:	https://ueaeprints.uea.ac.uk/id/eprint/21341
DOI:	10.1021/ja109581t

Actions (login required)

View Item