1N9C

Structure and dynamics of reduced Bacillus pasteurii cytochrome c: oxidation state dependent properties and implications for electron transfer processes

1N9C の概要

• エントリーDOI: 10.2210/pdb1n9c/pdb
• 関連するPDBエントリー: 1K3G
• NMR情報: BMRB: 5597
• 分子名称: Cytochrome c-553, HEME C (2 entities in total)
• 機能のキーワード: cytochrome c, respiration, electron transfer, redox, electron transport
• 由来する生物種: Sporosarcina pasteurii
• 細胞内の位置: Cell membrane; Peripheral membrane protein: P82599
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7734.44

構造登録者

Bartalesi, I.,Bertini, I.,Rosato, A. (登録日: 2002-11-23, 公開日: 2003-02-04, 最終更新日: 2024-10-09)

主引用文献

Bartalesi, I.,Bertini, I.,Rosato, A.
Structure and dynamics of reduced Bacillus pasteurii cytochrome c: oxidation state dependent properties and implications for electron transfer processes
Biochemistry, 42:739-745, 2003

PubMed Abstract: The solution structure of reduced Bacillus pasteurii cytochrome c, which has only 71 amino acids, has been determined by NMR to an RMSD of 0.46 +/- 0.08 A for all backbone atoms and 0.79 +/- 0.08 A for all heavy atoms and refined through restrained energy minimization. The target function out of 1645 constraints is 0.52 +/- 0.11 A(2), and the penalty function is 66 +/- 12 kJ mol(-)(1). The structure appears very similar to that in the oxidized state, only Trp87 and the propionates showing significant differences. The mobility was investigated through (15)N R(1) and R(2) relaxation rates, (15)N-(1)H NOE, and (1)H/(2)H exchange. It is found that the oxidized form is generally more mobile than the reduced one. By comparing the redox-state dependence of the structural/dynamic properties of Fe-S proteins, cytochrome c, and blue copper proteins, hints are provided for a better comprehension of the electron transfer processes.

PubMed: 12534286
DOI: 10.1021/bi0266028

実験手法

SOLUTION NMR