Heme orientation affects holo‐myoglobin folding and unfolding kinetics 1

FEBS Letters

Moczygemba, Charmaine¹  Guidry, Jesse¹  Wittung-Stafshede, Pernilla¹ 

[1] Department of Chemistry, Tulane University, 6832 St. Charles Avenue, New Orleans, LA 70118-5698, USA

关键词: Protein folding;    Myoglobin;    Stopped-flow mixing;    Heme protein;   

DOI  :  10.1016/S0014-5793(00)01319-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Native myoglobin (Mb) consists of two populations which differ in the orientation of the heme by 180° rotation (as verified by nuclear magnetic resonance) but have identical absorption spectra and equilibrium–thermodynamic stability. Here, we report that these two fractions of native oxidized Mb (from horse) both unfold and refold (chemical denaturant, pH 7, 20°C) in two parallel kinetic reactions with rate constants differing 10-fold. In accord, the oxidized heme remains coordinated to unfolded horse Mb in up to 4 M guanidine hydrochloride (pH 7, 20°C).

【 授权许可】

Unknown