Interaction of Yeast Iso-1-cytochrome c with Cytochrome c Peroxidase Investigated by [15N,1H] Heteronuclear NMR Spectroscopy

The interaction of yeast iso-1-cytochrome c with its physiological redox partner cytochrome c peroxidase has been investigated using heteronuclear NMR techniques. Chemical shift perturbations for both 15N and 1H nuclei arising from the interaction of isotopically enriched 15N cytochrome c with cytoc...

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Veröffentlicht in:	Biochemistry (Easton) 2001-06, Vol.40 (24), p.7069-7076
Hauptverfasser:	Worrall, Jonathan A. R, Kolczak, Urszula, Canters, Gerard W, Ubbink, Marcellus
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites Cytochrome c Group - chemistry Cytochrome c Group - metabolism Cytochrome-c Peroxidase - chemistry Cytochrome-c Peroxidase - metabolism Cytochromes c Ferric Compounds - chemistry Ferrous Compounds - chemistry Isoenzymes - chemistry Isoenzymes - metabolism Nitrogen Isotopes Nuclear Magnetic Resonance, Biomolecular - methods Oxidation-Reduction Protons Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae Proteins Thermodynamics
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