1GIW

SOLUTION STRUCTURE OF REDUCED HORSE HEART CYTOCHROME C, NMR, MINIMIZED AVERAGE STRUCTURE

1GIW の概要

• エントリーDOI: 10.2210/pdb1giw/pdb
• NMR情報: BMRB: 4189
• 分子名称: CYTOCHROME C, HEME C (2 entities in total)
• 機能のキーワード: electron transport, cytochrome c
• 由来する生物種: Equus caballus (horse)
• 細胞内の位置: Mitochondrion matrix: P00004
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12344.10

構造登録者

Banci, L.,Bertini, I.,Huber, J.G.,Spyroulias, G.A.,Turano, P. (登録日: 1998-06-17, 公開日: 1998-12-09, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

SOLUTION NMR