hexacyanocobaltate-(iii) and 4-chloro-3-5-dinitrobenzoate

hexacyanocobaltate-(iii) has been researched along with 4-chloro-3-5-dinitrobenzoate* in 1 studies

Other Studies

1 other study(ies) available for hexacyanocobaltate-(iii) and 4-chloro-3-5-dinitrobenzoate

Article	Year
The modulation of cytochrome c electron self-exchange by site-specific chemical modification and anion binding. FEBS letters, 1986, Sep-29, Volume: 206, Issue:1 The site-specific chemical modification of horse heart cytochrome c at Lys-13 and -72 using 4-chloro-3,5-dinitrobenzoic acid (CDNB) increases the electron self-exchange rate of the protein. In the presence of 0.24 M cacodylate (pH* 7.0) the electron self-exchange rate constants, kex, measured by a 1H NMR saturation transfer method at 300 K, are 600, 6 X 10(3) and 6 X 10(4) M-1 X s-1 for native, CDNP-K13 and CDNP-K72 cytochromes c respectively. Repulsive electrostatic interactions, which inhibit cytochrome c electron self-exchange, are differentially affected by modification. Measurements of 1H NMR line broadening observed with partially oxidised samples of native cytochrome c show that ATP and the redox inert multivalent anion Co(CN)3-6 catalyse electron self-exchange. At saturation a limiting value of approximately 1.4 X 10(5) M-1 X s-1 is observed for both anions. Topics: Adenosine Triphosphate; Anions; Cacodylic Acid; Chemical Phenomena; Chemistry; Chlorobenzoates; Cobalt; Cyanides; Cytochrome c Group; Electron Transport; Lysine; Magnetic Resonance Spectroscopy	1986

Article

Year

The modulation of cytochrome c electron self-exchange by site-specific chemical modification and anion binding.

FEBS letters, 1986, Sep-29, Volume: 206, Issue:1

The site-specific chemical modification of horse heart cytochrome c at Lys-13 and -72 using 4-chloro-3,5-dinitrobenzoic acid (CDNB) increases the electron self-exchange rate of the protein. In the presence of 0.24 M cacodylate (pH* 7.0) the electron self-exchange rate constants, kex, measured by a 1H NMR saturation transfer method at 300 K, are 600, 6 X 10(3) and 6 X 10(4) M-1 X s-1 for native, CDNP-K13 and CDNP-K72 cytochromes c respectively. Repulsive electrostatic interactions, which inhibit cytochrome c electron self-exchange, are differentially affected by modification. Measurements of 1H NMR line broadening observed with partially oxidised samples of native cytochrome c show that ATP and the redox inert multivalent anion Co(CN)3-6 catalyse electron self-exchange. At saturation a limiting value of approximately 1.4 X 10(5) M-1 X s-1 is observed for both anions.

Topics: Adenosine Triphosphate; Anions; Cacodylic Acid; Chemical Phenomena; Chemistry; Chlorobenzoates; Cobalt; Cyanides; Cytochrome c Group; Electron Transport; Lysine; Magnetic Resonance Spectroscopy

1986