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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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 Urheber:
Kroneck, P. M. H.1, Autor
Antholine, W. E.2, Autor
Koteich, H.2, Autor
Kastrau, D. H. W.1, Autor
Neese, F.1, Autor           
Zumft, W. G.3, Autor
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              

Inhalt

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Schlagwörter: Electron Paramagnetic Resonance; Euler Angle; Hyperfine Coupling; Paracoccus Denitrificans; Bioinorganic Chemistry
 Zusammenfassung: 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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Sprache(n): eng - English
 Datum: 1993
 Publikationsstatus: Erschienen
 Seiten: 8
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1007/978-94-011-6875-5_33
 Art des Abschluß: -

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Titel: Bioinorganic Chemistry of Copper
Genre der Quelle: Buch
 Urheber:
Karlin, Kenneth D.1, Herausgeber
Tyeklár, Zoltán1, Autor
Affiliations:
1 Department of Chemistry, Johns Hopkins University, Baltimore, Maryland, USA, ou_persistent22            
Ort, Verlag, Ausgabe: New York : Chapman and Hall, Inc.
Seiten: - Band / Heft: - Artikelnummer: - Start- / Endseite: 419 - 426 Identifikator: ISBN: 978-94-011-6877-9