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https://hdl.handle.net/20.500.14279/1551
Title: | Fourier transform infrared evidence for a ferric six-coordinate nitrosylheme b 3 complex of cytochrome cbb 3 oxidase from Pseudomonas stutzeri at ambient temperature |
Authors: | Stavrakis, Stavros Pinakoulaki, Eftychia Varotsis, Constantinos |
metadata.dc.contributor.other: | Σταυράκης, Σταύρος Πινακουλάκη, Ευτυχία Βαρώτσης, Κωνσταντίνος |
Major Field of Science: | Natural Sciences |
Field Category: | Chemical Sciences |
Keywords: | Fourier transform infrared spectroscopy;Organometallic chemistry;Chemical bonds;Dissociation;Nitrogen oxides;Oxidation |
Issue Date: | 21-Nov-2002 |
Source: | Journal of physical chemistry B, 2002, vol. 106, no. 50, pp. 12860-12862 |
Volume: | 106 |
Issue: | 50 |
Start page: | 12860 |
End page: | 12862 |
Journal: | Journal of Physical Chemistry B |
Abstract: | We report the first vibrational study of NO bound to an oxidized heme-copper oxidase. Cytochrome cbb 3 oxidase from P. stutzeri reduces both O 2 and NO to H 2O and N 2O, respectively. The ferric nitrosyl complex of cbb 3 exhibits v(N-O) at 1903 cm -1. This frequency is very similar to v(NO) of nitric oxide reductase, the acidic form of Met Mb-NO, but 18 cm -1 lower than that of neutral Met Mb-NO. By monitoring the NO intensity, we estimate that NO dissociates from the heme b 3 pocket, without binding to Cu B, with k = 1.8 × 10 -3 s -1. Therefore, NO binding occurs at the heme site and not at Cu B, generating a nitrosonium Cu B 1+-NO + species as proposed recently (Torres; J.; Cooper, C.E.; Wilson, M.T. J. Biol. Chem. 1998, 273, 8756-8766). The coordination of NO to cbb 3 oxidase and to nitric oxide reductase and Mb is compared and discussed |
URI: | https://hdl.handle.net/20.500.14279/1551 |
ISSN: | 10895647 |
DOI: | 10.1021/jp026763l |
Rights: | © American Chemical Society Attribution-NonCommercial-NoDerivs 3.0 United States |
Type: | Article |
Affiliation: | University of Crete |
Affiliation : | University of Oklahoma |
Publication Type: | Peer Reviewed |
Appears in Collections: | Άρθρα/Articles |
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