Please use this identifier to cite or link to this item: https://hdl.handle.net/20.500.14279/1308
Title: Nitric-oxide reductase: structure and properties of the catalytic site from resonance Raman scattering
Authors: Pinakoulaki, Eftychia 
Gemeinhardt, Sabine 
Varotsis, Constantinos 
metadata.dc.contributor.other: Πινακουλάκη, Ευτυχία
Βαρώτσης, Κωνσταντίνος
Major Field of Science: Natural Sciences
Field Category: NATURAL SCIENCES
Keywords: Biochemistry;Ligands;Deuterium;Enzymes;Nitrogen oxides;Photodissociation;Photochemistry;Raman spectroscopy
Issue Date: 26-Feb-2002
Source: Journal of biological chemistry, 2002, vol. 277, no. 26, pp. 23407-23413
Volume: 277
Issue: 26
Start page: 23407
End page: 23413
Journal: Journal of Biological Chemistry 
Abstract: We have applied resonance Raman spectroscopy to investigate the properties of the dinuclear center of oxidized, reduced, and NO-bound nitric-oxide reductase from Paracoccus denitrificans. The spectra of the oxidized enzyme show two distinct vas(Fe-O-Fe) modes at 815 and 833 cm-1 of the heme/non-heme diiron center. The splitting of the Fe-O-Fe mode suggests that two different conformations (open and closed) are present in the catalytic site of the enzyme. We find evidence from deuterium exchange experiments that in the dominant conformation (833 cm-1 mode, closed), the Fe-O-Fe unit is hydrogen-bonded to distal residue(s). The ferric nitrosyl complex of nitric-oxide reductase exhibits the v(Fe3+-NO) and v(N-O) at 594 and 1904 cm-1, respectively. The nitrosyl species we detect is photolabile and can be photolyzed to generate a new form of oxidized enzyme in which the proximal histidine is ligated to heme b3, in contrast to the resting form. Photodissociation of the NO ligand yields a five-coordinate high-spin heme b3. Based on the findings reported here, the structure and properties of the dinuclear center of nitricoxide reductase in the oxidized, reduced, and NO-bound form as well as its photoproduct can be described with certainty
URI: https://hdl.handle.net/20.500.14279/1308
ISSN: 00219258
DOI: 10.1074/jbc.M201913200
Rights: © The American Society for Biochemistry and Molecular Biology
Attribution-NonCommercial-NoDerivs 3.0 United States
Type: Article
Affiliation: University of Crete 
Affiliation : University of Crete 
European Molecular Biology Laboratory 
Publication Type: Peer Reviewed
Appears in Collections:Άρθρα/Articles

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