Heme orientation affects holo-myoglobin folding and unfolding kinetics1
作者： Charmaine Moczygemba , Jesse Guidry , Pernilla Wittung-Stafshede
DOI: 10.1016/S0014-5793(00)01319-3
关键词:
摘要: Native myoglobin (Mb) consists of two populations which differ in the orientation heme by 180° rotation (as verified nuclear magnetic resonance) but have identical absorption spectra and equilibrium–thermodynamic stability. Here, we report that these fractions native oxidized Mb (from horse) both unfold refold (chemical denaturant, pH 7, 20°C) parallel kinetic reactions with rate constants differing 10-fold. In accord, remains coordinated to unfolded horse up 4 M guanidine hydrochloride (pH 20°C).
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