ISSN:
0749-1581
Keywords:
1H NMR
;
NOESY
;
Cytochrome c
;
Trimethylphosphine
;
Electron transfer
;
Self-exchange
;
Chemistry
;
Analytical Chemistry and Spectroscopy
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
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 (T1) measurement. The rate is 7.5 × 103 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.
Additional Material:
2 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/mrc.1260311307
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