1H-NMR investigation of yeast cytochrome c. Interaction with the corresponding specific reductase (L-lactate cytochrome).
Biochem Biophys Res Commun
; 145(3): 1098-104, 1987 Jun 30.
Article
em En
| MEDLINE
| ID: mdl-3038091
ABSTRACT
1H-NMR spectroscopy has been used to study the modifications of certain characteristic resonances of the Hansenula anomala yeast cytochrome c on binding to its specific reductase (flavocytochrome b2) or to the isolated cytochrome domain obtained from the entire molecule. Normal titration curves are observed for the resonances at 37.8 ppm assigned to heme c methyl 8 and at 19.4 ppm, line of cytochrome b2 spectrum. In contrast, the shifts near 3.2 and 3.4 ppm for trimethyl-lysine resonances of this cytochrome c present abnormal titration curves, saturation being apparently reached at low molar (cytochrome b2)/(cytochrome c) ratio. An interpretation is proposed in terms of shifts due to local conformational transitions induced by reductase binding but not rapidly reversible upon dissociation.
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01-internacional
Base de dados:
MEDLINE
Assunto principal:
Pichia
/
Grupo dos Citocromos c
/
Saccharomycetales
/
L-Lactato Desidrogenase
Idioma:
En
Ano de publicação:
1987
Tipo de documento:
Article