NMR double resonance study of azide binding to cytochrome c

Autor:	D. Concar, R. J. P. Williams, G. R. Moore, Wen-Xia Tang
Rok vydání:	2010
Předmět:	biology Chemistry Cytochrome c Inorganic chemistry General Chemistry Resonance (chemistry) Crystallography chemistry.chemical_compound Lower affinity medicine biology.protein Ferric Azide Hemeproteins Equilibrium constant medicine.drug
Zdroj:	Chinese Journal of Chemistry. 10:40-44
ISSN:	1001-604X
DOI:	10.1002/cjoc.19920100108
Popis:	Equilibrium constants for the binding of azide to ferri-cytochrome c at temperature range-of 305–325 K were determined at pH =7 by using 1H double resonance method. Thermodynamic values (ΔH° =-34.5 kJ/mol, ΔS°=-100 J/mol) were obtained from van't Hoff's relation and were compared with those for azide binding to other ferric hemeproteins. The reason of lower affinity of cytochrome c for azide was discussed.
Databáze:	OpenAIRE
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