2GIW

SOLUTION STRUCTURE OF REDUCED HORSE HEART CYTOCHROME C, NMR, 40 STRUCTURES

Summary for 2GIW

• Entry DOI: 10.2210/pdb2giw/pdb
• Descriptor: CYTOCHROME C, HEME C (2 entities in total)
• Functional Keywords: electron transport, cytochrome c
• Biological source: Equus caballus (horse)
• Cellular location: Mitochondrion matrix: P00004
• Total number of polymer chains: 1
• Total formula weight: 12344.10

Authors

Banci, L.,Bertini, I.,Huber, J.G.,Spyroulias, G.A.,Turano, P. (deposition date: 1998-06-25, release date: 1998-12-09, Last modification date: 2024-10-09)

Primary citation

Banci, L.,Bertini, I.,Huber, J.G.,Spyroulias, G.A.,Turano, P.
Solution structure of reduced horse heart cytochrome c.
J.Biol.Inorg.Chem., 4:21-31, 1999

PubMed Abstract: In the frame of a broad study on the structural differences between the two redox forms of cytochromes to be related to the electron transfer process, the NMR solution structure of horse heart cytochrome c in the reduced form has been determined. The structural data obtained in the present work are compared to those already available in the literature on the same protein and the presence of conformational differences is discussed in the light of the experimental method employed for the structure determination. Redox-state dependent changes are analyzed and in particular they are related to the role of propionate-7 of the heme. Also some hydrogen bonds are changed upon reduction of the heme iron. A substantial similarity is observed for the backbone fold, independently of the oxidation state. At variance, some meaningful differences are observed in the orientation of a few side chains. These changes are related to those found in the case of the highly homologous cytochrome c from Saccharomyces cerevisiae. The exchangeability of the NH protons has been investigated and found to be smaller than in the case of the oxidized protein. We think that this is a characteristic of reduced cytochromes and that mobility is a medium for molecular recognition in vivo.

PubMed: 10499099
DOI: 10.1007/s007750050285

Experimental method

SOLUTION NMR