Crystal structure of the oxidized cytochrome c 2 from Blastochloris viridis

FEBS Letters

Sogabe, Satoshi²  Miki, Kunio¹ 

[1] Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan;Research Laboratory of Resources Utilization, Tokyo Institute of Technology, 4259 Nagatsuta, Yokohama, Kanagawa 226, Japan

关键词: Cytochrome c 2;    Oxidation state;    Crystal structure;    Electron transfer;    RC;    reaction center;   

DOI  :  10.1016/S0014-5793(01)02179-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The crystal structure of the oxidized cytochrome c ₂ from Blastochloris (formerly Rhodopseudomonas) viridis was determined at 1.9 Å resolution. Structural comparison with the reduced form revealed significant structural changes according to the oxidation state of the heme iron. Slight perturbation of the polypeptide chain backbone was observed, and the secondary structure and the hydrogen patterns between main-chain atoms were retained. The oxidation state-dependent conformational shifts were localized in the vicinity of the methionine ligand side and the propionate group of the heme. The conserved segment of the polypeptide chain in cytochrome c and cytochrome c ₂ exhibited some degree of mobility, interacting with the heme iron atom by the hydrogen bond network. These results indicate that the movement of the internal water molecule conserved in various c-type cytochromes drives the adjustments of side-chain atoms of nearby residue, and the segmental temperature factor changes along the polypeptide chain.

【 授权许可】

Unknown