1lc1
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Solution Structure Of Reduced Horse Heart Cytochrome c in 30% Acetonitrile Solution, NMR Minimized Average Structure
OverviewOverview
The complete solution structure of ferrocytochrome c in 30% acetonitrile/70% water has been determined using high-field 1D and 2D (1)H NMR methods and deposited in the Protein Data Bank with codes 1LC1 and 1LC2. This is the first time a complete solution protein structure has been determined for a protein in nonaqueous media. Ferrocyt c retains a native protein secondary structure (five alpha-helices and two omega loops) in 30% acetonitrile. H18 and M80 residues are the axial heme ligands, as in aqueous solution. Residues believed to be axial heme ligands in the alkaline-like conformers of ferricyt c, specifically H33 and K72, are positioned close to the heme iron. The orientations of both heme propionates are markedly different in 30% acetonitrile/70% water. Comparative structural analysis of reduced cyt c in 30% acetonitrile/70% water solution with cyt c in different environments has given new insight into the cyt c folding mechanism, the electron transfer pathway, and cell apoptosis.
About this StructureAbout this Structure
1LC1 is a Single protein structure of sequence from Equus caballus with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Structure-function relationship of reduced cytochrome c probed by complete solution structure determination in 30% acetonitrile/water solution., Sivakolundu SG, Mabrouk PA, J Biol Inorg Chem. 2003 May;8(5):527-39. Epub 2003 Feb 15. PMID:12764601
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