A study of the electron transfer properties of the heme undecapeptide from cytochrome c by 1H nmr spectroscopy.
Nuclear magnetic resonance (nmr) spectroscopy has been used to investigate the heme undecapeptide from cytochrome c. Assignments of resonances to specific residues have been made based on spin decoupling, redox titration, and the pH and temperature dependence of resonance lines. An outline structure is presented based on the assignments, secondary shift data, and the x-ray crystal structure of cytochrome c. An equation is derived to relate the width of an nmr line during a redox titration to the percentage of each oxidation state. Using this equation the self-exchange rate constant for electron transfer for the heme peptide is 1.3 x 10(7) M-1 sec-1 at 330 degrees K. Discussion of the self-exchange rate constants of cytochrome c, cytochrome c3, and cytochrome c551 is related to this constant for the heme undecapeptide.
D000818:Animals; D003574:Cytochrome c Group / Q000378:metabolism*; D004579:Electron Transport; D006418:Heme / Q000031:analogs & derivatives*; D006427:Hemin / Q000378:metabolism*; D006736:Horses; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D009206:Myocardium; D009842:Oligopeptides / Q000378:metabolism*; D010084:Oxidation-Reduction
D003574:Cytochrome c Group; D009842:Oligopeptides; C013994:ferri-heme undecapeptide; D006418:Heme; D006427:Hemin