Heme orientation affects holo-myoglobin folding and unfolding kinetics

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 (fr...

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Bibliographic Details
Published in:FEBS letters 2000-03, Vol.470 (2), p.203-206
Main Authors: Moczygemba, Charmaine, Guidry, Jesse, Wittung-Stafshede, Pernilla
Format: Article
Language:English
Subjects:
Animals
Apoproteins - chemistry
Apoproteins - metabolism
Circular Dichroism
Dose-Response Relationship, Drug
Fluorescence
Guanidine - pharmacology
Heme - metabolism
Heme protein
Horses
Kinetics
Metmyoglobin - chemistry
Metmyoglobin - metabolism
Myoglobin
Myoglobin - chemistry
Myoglobin - metabolism
Protein Denaturation - drug effects
Protein Folding
Protein Renaturation
Rotation
Stopped-flow mixing
Thermodynamics
Tryptophan - metabolism
Whales
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Description
Summary: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).
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(00)01319-3