title: NMR study of the alkaline isomerization of ferricytochrome c.
abstract: The pH-induced isomerization of horse heart cytochrome c has been studied by 1H NMR. We find that the transition occurring in D2O with a pKa measured as 9.5 +/- 0.1 is from the native species to a mixture of two basic forms which have very similar NMR spectra. The heme methyl peaks of these two forms have been assigned by 2D exchange NMR. The forward rate constant (native to alkaline cytochrome c) has a value of 4.0 +/- 0.6 s-1 at 27 degrees C and is independent of pH; the reverse rate constant is pH-dependent. The activation parameters are delta H not equal to = 12.8 +/- 0.8 kcal.mol1, delta S not equal to = -12.9 +/- 2.0 e.u. for the forward reaction and delta H not equal to = 6.0 +/- 0.3 kcal.mol-1, delta S not equal to = -35.1 +/- 1.3 e.u. for the reverse reaction (pH* = 9.28). delta H degree and delta S degree for the isomerization are 6.7 +/- 0.6 kcal.mol-1 and 21.9 +/- 1.0 e.u., respectively.
authors.affiliation: Department of Chemistry and Laboratory, Georgia State University, Atlanta 30303.
authors.forename: X L
authors.initials: XL
authors.lastname: Hong
authors.forename: D W
authors.initials: DW
authors.lastname: Dixon
mesh_terms: D003574:Cytochrome c Group / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007536:Isomerism; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D013696:Temperature; D013816:Thermodynamics
chemical_list: D003574:Cytochrome c Group