Kinetic studies on the effect of the heme iron(III) on the protein folding of ferricytochrome c.
作者： R.W. Henkens , S.R. Turner
DOI: 10.1016/S0021-9258(19)86858-8
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摘要: Abstract The three-dimensional conformation of ferricytochrome c results from specific folding the polypeptide chain around covalently bound heme so that His-18 and Met-80 are axially coordinated to Fe(III). Fe(III)-free, porphyrin protein has an intrinsic viscosity, sedimentation coefficient, circular dichroism indicative a compact, globular comparable holoprotein. Both reversibly denatured by guanidinium chloride. Refolding occurs in essentially single, exceptionally rapid kinetic phase (tau = 14 ms, 0.75 M chloride, pH 6.5, 25 degrees C); whereas refolding two slower phases (TAU 1 0.10 S, TAU 2 20 S) UNDER COMPARABLE CONDITIONS. presence Fe(III) metalloporphyrin thus major effect on kinetics. slow is evidently due this not cis-trans isomerism peptide bond proline residues as been suggested.
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