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  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. (1993). The EPR-Detectable Copper of Nitrous Oxide Reductase as a Model for CuA 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.

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 Creators:
Kroneck, P. M. H.1, Author
Antholine, W. E.2, Author
Koteich, H.2, Author
Kastrau, D. H. W.1, Author
Neese, F.1, Author              
Zumft, W. G.3, Author
Affiliations:
1Fakultät für Biologie, Universität Konstanz, Konstanz, Germany, ou_persistent22              
2Biophysics Research Institute, Medical College of Wisconsin, Milwaukee, USA, ou_persistent22              
3Lehrstuhl für Mikrobiologie, Universität Karlsruhe, Karlsruhe, Germany, ou_persistent22              

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Free keywords: Electron Paramagnetic Resonance; Euler Angle; Hyperfine Coupling; Paracoccus Denitrificans; Bioinorganic Chemistry
 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

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Language(s): eng - English
 Dates: 1993
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1007/978-94-011-6875-5_33
 Degree: -

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Title: Bioinorganic Chemistry of Copper
Source Genre: Book
 Creator(s):
Karlin, Kenneth D.1, Editor
Tyeklár, Zoltán1, Author
Affiliations:
1 Department of Chemistry, Johns Hopkins University, Baltimore, Maryland, USA, ou_persistent22            
Publ. Info: New York : Chapman and Hall, Inc.
Pages: - Volume / Issue: - Sequence Number: - Start / End Page: 419 - 426 Identifier: ISBN: 978-94-011-6877-9