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EPR Characterisation of the Ferrous Nitrosyl Complex Formed within the Oxygenase Domain of NO Synthase.

Santolini, J; Maréchal, A; Boussac, A; Dorlet, P; (2013) EPR Characterisation of the Ferrous Nitrosyl Complex Formed within the Oxygenase Domain of NO Synthase. Chembiochem , 14 (14) pp. 1852-1857. 10.1002/cbic.201300233. Green open access

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Abstract

Nitric oxide is produced in mammals by a class of enzymes called NO synthases (NOSs). It plays a central role in cellular signalling but also has deleterious effects, as it leads to the production of reactive oxygen and nitrogen species. NO forms a relatively stable adduct with ferrous haem proteins, which, in the case of NOS, is also a key catalytic intermediate. Despite extensive studies on the ferrous nitrosyl complex of other haem proteins (in particular myoglobin), little characterisation has been performed in the case of NOS. We report here a temperature-dependent EPR study of the ferrous nitrosyl complex of the inducible mammalian NOS and the bacterial NOS-like protein from Bacillus subtilis. The results show that the overall behaviours are similar to those observed for other haem proteins, but with distinct ratios between axial and rhombic forms in the case of the two NOS proteins. The distal environment appears to control the existence of the axial form and the evolution of the rhombic form.

Type: Article
Title: EPR Characterisation of the Ferrous Nitrosyl Complex Formed within the Oxygenase Domain of NO Synthase.
Open access status: An open access version is available from UCL Discovery
DOI: 10.1002/cbic.201300233
Publisher version: http://dx.doi.org/10.1002/cbic.201300233
Additional information: © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. Full text made available to UCL Discovery by kind permission of Wiley.
Keywords: EPR spectroscopy, NO-synthases, heme proteins, nitrosyl complexes
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology
URI: https://discovery.ucl.ac.uk/id/eprint/1404814
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