Electron‐transfer self‐exchange of trimethylphosphine‐modified cytochrome  c : NMR study and kinetics using spin‐lattice relaxation times | Zendy

Legrand Nathalie | Zendy; Bondon Arnaud | Zendy; Simonneaux Gérard | Zendy; Schejter Abel | Zendy

Premium

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 .

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research