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NMR double resonance study of azide binding to cytochrome c
Author(s) -
Tang WenXia,
Concar D.,
Moore G. R.,
Williams R. J. P.
Publication year - 1992
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.19920100108
Subject(s) - chemistry , azide , resonance (particle physics) , ferric , cytochrome , proton nmr , cytochrome c , stereochemistry , inorganic chemistry , organic chemistry , enzyme , biochemistry , atomic physics , physics , mitochondrion
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 1 H 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.