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Substrate Binding to a Nitrite Reductase Induces a Spin Transition
Citation key ISI:000276889100042
Author 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
Pages 5563-5566
Year 2010
ISSN 1520-6106
DOI 10.1021/jp9118502
Address 1155 16TH ST, NW, WASHINGTON, DC 20036 USA
Journal J. Phys. Chem. B
Volume 114
Number 16
Month APR 29
Publisher AMER CHEMICAL SOC
Abstract 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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