1LC2

Solution Structure Of Reduced Horse Heart Cytochrome c in 30% Acetonitrile Solution, NMR 30 Structures

Summary for 1LC2

• Entry DOI: 10.2210/pdb1lc2/pdb
• Related: 1LC1
• NMR Information: BMRB: 5372
• Descriptor: CYTOCHROME C, HEME C (2 entities in total)
• Functional Keywords: cytochrome c, organic solvent, electron transport
• Biological source: Equus caballus (horse)
• Cellular location: Mitochondrion matrix: P00004
• Total number of polymer chains: 1
• Total formula weight: 12344.10

Authors

Sivakolundu, S.G.,Mabrouk, P.A. (deposition date: 2002-04-04, release date: 2003-06-03, Last modification date: 2024-10-30)

Primary citation

Sivakolundu, S.G.,Mabrouk, P.A.
Structure function relationship of reduced cytochrome c probed by complete solution structure determination in 30% acetonitrile/water solution
J.BIOL.INORG.CHEM., 8:527-539, 2003

PubMed Abstract: 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.

PubMed: 12764601

Experimental method

SOLUTION NMR