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Daskalakis V, Ohta T, Kitagawa T, et al. Structure and properties of the catalytic site of nitric oxide reductase at ambient temperature. Biochim Biophys Acta. 2015;1847(10):1240-4doi: 10.1016/j.bbabio.2015.06.014.
Daskalakis, V., Ohta, T., Kitagawa, T., & Varotsis, C. (2015). Structure and properties of the catalytic site of nitric oxide reductase at ambient temperature. Biochimica et biophysica acta, 1847(10), 1240-4. https://doi.org/10.1016/j.bbabio.2015.06.014
Daskalakis, Vangelis, et al. "Structure and properties of the catalytic site of nitric oxide reductase at ambient temperature." Biochimica et biophysica acta vol. 1847,10 (2015): 1240-4. doi: https://doi.org/10.1016/j.bbabio.2015.06.014
Daskalakis V, Ohta T, Kitagawa T, Varotsis C. Structure and properties of the catalytic site of nitric oxide reductase at ambient temperature. Biochim Biophys Acta. 2015 Oct;1847(10):1240-4. doi: 10.1016/j.bbabio.2015.06.014. Epub 2015 Jul 02. PMID: 26140941.
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Biochim Biophys Acta. 2015 Oct;1847(10):1240-4. doi: 10.1016/j.bbabio.2015.06.014. Epub 2015 Jul 02.

Structure and properties of the catalytic site of nitric oxide reductase at ambient temperature.

Biochimica et biophysica acta

Vangelis Daskalakis, Takehiro Ohta, Teizo Kitagawa, Constantinos Varotsis

Affiliations

  1. Department of Environmental Science and Technology, Cyprus University of Technology, P.O. Box 50329, 3603 Lemesos, Cyprus.
  2. Picobiology Institute, Graduate School of Life Science, University of Hyogo, Hyogo 678-1297, Japan.
  3. Department of Environmental Science and Technology, Cyprus University of Technology, P.O. Box 50329, 3603 Lemesos, Cyprus. Electronic address: [email protected].

PMID: 26140941 DOI: 10.1016/j.bbabio.2015.06.014

Abstract

Nitric oxide reductase (Nor) is the third of the four enzymes of bacterial denitrification responsible for the catalytic formation of laughing gas (N2O). Here we report the detection of the hyponitrite (HO-N=N-O(-)) species (νN-N=1332cm(-1)) in the heme b3 Fe-FeB dinuclear center of Nor from Paracoccus denitrificans. We have also applied density functional theory (DFT) to characterize the bimetallic-bridging hyponitrite species in the reduction of NO to N2O by Nor and compare the present results with those recently reported for the N-N bond formation in the ba3 and caa3 oxidoreductases from Thermus thermophilus.

Copyright © 2015. Published by Elsevier B.V.

Keywords: Density functional theory; Heme proteins; Hyponitrite; Oxidoreductases; UV Raman spectroscopy

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