400 - A reexamination of the temperature dependence of spectral bands in the 600–780 nm region of cytochrome c
Author:
Publisher
Elsevier BV
Subject
Electrochemistry,Physical and Theoretical Chemistry,Biophysics
Reference16 articles.
1. The 695-mμ Band of Ferricytochrome c and Its Relationship to Protein Conformation*
2. Studies on Ferricytochrome c. 2. A Correlation between Reducibility and the Possession of the 695 nm Absorption Band of Ferricytochrome c
3. Interaction of cytochrome c and the phosphoprotein phosvitin. Formation of a complex with an intact 695-m.mu. absorption band
4. A method for investigating the effect of temperature on the 695 nm band of insoluble cytochrome c
5. Thermodynamic studies of the opening of the heme crevice of ferricytochrome c
Cited by 5 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. The effects of temperature and electrolyte on the redox potential of cytochrome c at a chemically modified microband gold electrode;Electrochimica Acta;1995-06
2. Temperature and electrolyte effects on the electron-transfer reactions of cytochrome c;Journal of the American Chemical Society;1985-12
3. 722—The effect of pH on the temperature dependence of the redox potential of horse heart cytochrome c at a bis(4-pyridyl)disulfide-modified gold electrode;Bioelectrochemistry and Bioenergetics;1984-12
4. Detection of a bulk water structure related conformational change in horse heart cytochrome c in Cl − −H 2 O solutions utilizing spectrofluoroelectrochemical techniques;Analytical Biochemistry;1984-05
5. Voltammetric response of horse heart cytochrome c at a gold electrode in the presence of sulfur bridged bipyridines;Journal of Electroanalytical Chemistry and Interfacial Electrochemistry;1982-11
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