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Title: Nitric-oxide reductase: structure and properties of the catalytic site from resonance Raman scattering
Authors: Pinakoulaki, Eftychia 
Gemeinhardt, Sabine
Varotsis, Constantinos 
Keywords: Biochemistry;Ligands;Deuterium;Enzymes;Nitrogen oxides;Photodissociation;Photochemistry;Raman spectroscopy
Issue Date: 2002
Publisher: American Society for Biochemistry and Molecular Biology
Source: Journal of biological chemistry, 2002, Volume 277, Issue 26, Pages 23407-23413
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
ISSN: 00219258
DOI: 10.1074/jbc.M201913200
Rights: © 2002 by The American Society for Biochemistry and Molecular Biology, Inc
Type: Article
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