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Electron‐transfer self‐exchange of trimethylphosphine‐modified cytochrome c : NMR study and kinetics using spin‐lattice relaxation times
Author(s) -
Legrand Nathalie,
Bondon Arnaud,
Simonneaux Gérard,
Schejter Abel
Publication year - 1993
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.1260311307
Subject(s) - chemistry , trimethylphosphine , kinetics , nuclear magnetic resonance spectroscopy , relaxation (psychology) , spin–lattice relaxation , electron transfer , spectroscopy , analytical chemistry (journal) , crystallography , inorganic chemistry , nuclear magnetic resonance , stereochemistry , organic chemistry , crystal structure , psychology , social psychology , physics , quantum mechanics , nuclear quadrupole resonance
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 .