The cytochrome c fold can be attained from a compact apo state by occupancy of a nascent heme binding site.

Journal article

NMR techniques and 8-anilino-1-napthalenesulphonate (ANS) binding studies have been used to characterize the apo state of a variant of cytochrome c(552) from Hydrogenobacter thermophilus. In this variant the two cysteines that form covalent thioether linkages to the heme group have been replaced by alanine residues (C11A/C14A). CD studies show that the apo state contains approximately 14% helical secondary structure, and measurements of hydrodynamic radii using pulse field gradient NMR method...

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Authors: Wain, R; Pertinhez, T; Tomlinson, E; Hong, L; Dobson, C

• Publication status: Published
• Journal: Journal of biological chemistry
• Volume: 276
• Issue: 49
• Pages: 45813-45817
• Publication date: 2001-12-01
• DOI: 10.1074/jbc.m107572200
• EISSN: 1083-351X
• ISSN: 0021-9258
• Language: English
• Keywords: Binding Sites; Protein Structure, Secondary; Cytochrome c Group; Spectrometry, Fluorescence; Nuclear Magnetic Resonance, Biomolecular; Bacteria; Circular Dichroism; Heme; Protein Folding