Recent NMR structural and dynamical data on partially folded forms of mono-heme cytochrome c provide a unifying picture of the behavior of the protein far from the native conditions and suggest useful hints to explain the redox dependent stability of the protein. A fragile hinge in the structure of mitochondrial cytochrome c is identified, which may not have correspondents in smaller type-1 cytochromes. Former spectroscopic and kinetic data are here discussed in terms of this new view.
Cytochrome c folding/unfolding: a unifying picture / I.Bertini; A.Rosato; P.Turano. - In: JOURNAL OF PORPHYRINS AND PHTHALOCYANINES. - ISSN 1088-4246. - STAMPA. - 8:(2004), pp. 238-245.
Cytochrome c folding/unfolding: a unifying picture
BERTINI, IVANO;ROSATO, ANTONIO;TURANO, PAOLA
2004
Abstract
Recent NMR structural and dynamical data on partially folded forms of mono-heme cytochrome c provide a unifying picture of the behavior of the protein far from the native conditions and suggest useful hints to explain the redox dependent stability of the protein. A fragile hinge in the structure of mitochondrial cytochrome c is identified, which may not have correspondents in smaller type-1 cytochromes. Former spectroscopic and kinetic data are here discussed in terms of this new view.
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