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• W1998034059 startingPage "1523" @default.
• W1998034059 abstract "To understand general aspects of stability and folding of c-type cytochromes, we have studied the folding characteristics of cytochrome c553 from Desulfovibrio vulgaris (Hildenborough). This cytochrome is structurally similar but lacks sequence homology to other heme proteins; moreover, it has an abnormally low reduction potential. Unfolding of oxidized and reduced cytochrome c553 by guanidine hydrochloride (GuHCl) was monitored by circular dichroism (CD) and Soret absorption; the same unfolding curves were obtained with both methods supporting that cytochrome c553 unfolds by an apparent two-state process. Reduced cytochrome c553 is 7(3) kJ/mol more stable than the oxidized form; accordingly, the reduction potential of unfolded cytochrome c553 is 100(20) mV more negative than that of the folded protein. In contrast to many other unfolded cytochrome c proteins, upon unfolding at pH 7.0 both oxidized and reduced heme in cytochrome c553 become high-spin. The lack of heme misligation in unfolded cytochrome c553 implies that its unfolded structure is less constrained than those of cytochromes c with low-spin, misligated hemes." @default.
• W1998034059 created "2016-06-24" @default.
• W1998034059 creator A5014446807 @default.
• W1998034059 date "1999-01-01" @default.
• W1998034059 modified "2023-09-29" @default.
• W1998034059 title "Equilibrium unfolding of a small low-potential cytochrome, cytochrome<i>c</i>₅₅₃from<i>Desulfovibrio vulgaris</i>" @default.
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• W1998034059 doi "https://doi.org/10.1110/ps.8.7.1523" @default.
• W1998034059 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2144372" @default.
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