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 HEC 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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