✦ LIBER ✦
Electron-transfer self-exchange of trimethylphosphine-modified cytochrome c: NMR study and kinetics using spin-lattice relaxation times
✍ Scribed by Nathalie Legrand; Arnaud Bondon; Gérard Simonneaux; Abel Schejter
- Publisher
- John Wiley and Sons
- Year
- 1993
- Tongue
- English
- Weight
- 395 KB
- Volume
- 31
- Category
- Article
- ISSN
- 0749-1581
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✦ Synopsis
Abstract
The binding of trimethylphosphine to the axial position of the haeme iron in modified cytochrome c by alkylation of methionine was studied by NMR spectroscopy. Electron self‐exchange was determined by spin‐lattice relaxation time (T~1~) measurement. The rate is 7.5 × 10^3^ 1 mol^−1^ s^−1^ at 25°C in 0.1 M phosphate buffer (pH 7.0). Two‐dimensional transfer spectroscopy was used to locate haeme methyl resonances in both iron(II) and iron(III) complexes of modified cytochrome c.