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Substrate Binding to a Nitrite Reductase Induces a Spin Transition
Zitatschlüssel ISI:000276889100042
Autor Martins, Gabriel and Rodrigues, Luisa and Cunha, Filipa M. and Matos, Daniela and Hildebrandt, Peter and Murgida, Daniel H. and Pereira, Ines A. C. and Todorovic, Smilja
Seiten 5563-5566
Jahr 2010
ISSN 1520-6106
DOI 10.1021/jp9118502
Adresse 1155 16TH ST, NW, WASHINGTON, DC 20036 USA
Journal J. Phys. Chem. B
Jahrgang 114
Nummer 16
Monat APR 29
Verlag AMER CHEMICAL SOC
Zusammenfassung The multiheme enzyme nitrite reductase catalyzes a 6-electron reduction of nitrite to ammonia. The reaction is initiated by substrate binding to the free axial position of the high spin penta-coordinated heme active site. The spin configuration of the resulting complex is crucial for discrimination between the heterolytic vs homolytic character of the cleavage of the N-O bond and, therefore, subsequent steps of the catalytic cycle. Here, we report the first experimental evidence, based on resonance Raman spectroscopy, that nitrite binding to the enzyme from D. vulgaris induces a transition from the high spin to the low spin configuration in the catalytic heme, thereby favoring the heterolytic route.
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