Title : Kinetic mechanism of cytochrome c folding: involvement of the heme and its ligands.

Pub. Date : 1994 Jun 7

PMID : 8204626






2 Functional Relationships(s)
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1 Under typical denaturing conditions (concentrated guanidine hydrochloride or urea near pH 7), one of the axial ligands, His 18, remains bound to the oxidized heme iron, but the second ligand, Met 80, is replaced by a non-native histidine ligand (His 26 or His 33 in horse cytochrome c). Histidine cytochrome c, somatic Equus caballus
2 Heme absorbance changes induced by rapid acidification of oxidized cytochrome c in 4.5 M guanidine hydrochloride from pH 7.8 to 4.6 or below exhibit two kinetic phases with rates of 110 and 25 s-1, attributed to the dissociation of non-native histidine ligands from the heme in the unfolded state. Histidine cytochrome c, somatic Equus caballus