The EPR-Detectable Copper of Nitrous Oxide Reductase as a Model for CuA in 
Cytochrome c Oxidase: A Multifrequency Electron Paramagnetic Resonance 
Investigation

Kroneck, P. M. H.; Antholine, W. E.; Koteich, H.; Kastrau, D. H. W.; Neese, F.; Zumft, W. G.

doi:10.1007/978-94-011-6875-5_33

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The EPR-Detectable Copper of Nitrous Oxide Reductase as a Model for Cu_A in Cytochrome c Oxidase: A Multifrequency Electron Paramagnetic Resonance Investigation

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Citation

Kroneck, P. M. H., Antholine, W. E., Koteich, H., Kastrau, D. H. W., Neese, F., & Zumft, W. G. (1993). The EPR-Detectable Copper of Nitrous Oxide Reductase as a Model for Cu_A in Cytochrome c Oxidase: A Multifrequency Electron Paramagnetic Resonance Investigation. In K. D. Karlin (Ed.), Bioinorganic Chemistry of Copper (pp. 419-426). New York: Chapman and Hall, Inc.

Cite as: https://hdl.handle.net/21.11116/0000-0007-CE54-3

Abstract

Nitrous oxide reductase (N₂OR) is the terminal reductase in a respiratory chain converting N₂O to N₂ in the denitrifying bacteria:

N₂O+2H⁺+2e⁻→N₂+H₂O ([1])

Principal aspects of the subject have been covered recently, and these reviews may be consulted for primary reference.^1,2 The high activity form of the enzyme from Pseudomonas stutzeri (N₂OR I) has two identical subunits, each carrying a mixed-valence [Cu(1.5)...Cu(1.5)], S = 1/2 complex.³ A catalytically inactive derivative of the enzyme (N₂OR V) has also the mixed-valence EPR-detectable site.^4,5