A general method for determining the electron self-exchange rates of blue copper proteins by longitudinal NMR relaxation.
A general NMR method is presented that allows a precise determination of the second-order rate constant, k(ese), for the electron self-exchange in blue copper proteins, from the longitudinal relaxation rates of the nuclei in the protein. The method relies on the use of partly oxidized (paramagnetic) samples of the protein. In contrast to previous NMR approaches for the determination of electron self-exchange rates, the applicability of the method extends beyond the slow-exchange limit, k(ese)c << R(ip), i = 1, 2, where c is the protein concentration, and R(ip) is the paramagnetic relaxation enhancement of the observed nuclei.
Jensen
Malene Ringkjøbing
MR
Department of Chemistry, University of Copenhagen, The H. C. Ørsted Institute, Universitetsparken 5, DK-2100 Copenhagen Ø, Denmark.
Hansen
D Flemming
DF
Led
Jens J
JJ
D001426:Bacterial Proteins / Q000737:chemistry*; D004583:Electrons; D007700:Kinetics; D008956:Models, Chemical; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010084:Oxidation-Reduction
D001426:Bacterial Proteins; C017079:mauC protein, Methylobacterium extorquens