NMR double resonance study of azide binding to cytochrome  c | Zendy

Tang WenXia | Zendy; Concar D. | Zendy; Moore G. R. | Zendy; Williams R. J. P. | Zendy

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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.

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