1GM4
OXIDISED STRUCTURE OF CYTOCHROME C3 FROM DESULFOVIBRIO DESULFURICANS ATCC 27774 at pH 7.6
1GM4 の概要
エントリーDOI | 10.2210/pdb1gm4/pdb |
関連するPDBエントリー | 1GMB 3CYR |
分子名称 | CYTOCHROME C3, HEME C, SULFATE ION, ... (4 entities in total) |
機能のキーワード | electron transport, cytochrome |
由来する生物種 | DESULFOVIBRIO DESULFURICANS |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 14188.55 |
構造登録者 | Bento, I.,Louro, R.,Matias, P.M.,Catarino, T.,Baptista, A.M.,Soares, C.M.,Carrondo, M.A.,Turner, D.L.,Xavier, A.V. (登録日: 2001-09-10, 公開日: 2002-09-05, 最終更新日: 2024-10-09) |
主引用文献 | Louro, R.O.,Bento, I.,Matias, P.M.,Catarino, T.,Baptista, A.M.,Soares, C.M.,Carrondo, M.A.,Turner, D.L.,Xavier, A.V. Conformational Component in the Coupled Transfer of Multiple Electrons and Protons in a Monomeric Tetraheme Cytochrome. J.Biol.Chem., 276:44044-, 2001 Cited by PubMed Abstract: Cell metabolism relies on energy transduction usually performed by complex membrane-spanning proteins that couple different chemical processes, e.g. electron and proton transfer in proton-pumps. There is great interest in determining at the molecular level the structural details that control these energy transduction events, particularly those involving multiple electrons and protons, because tight control is required to avoid the production of dangerous reactive intermediates. Tetraheme cytochrome c(3) is a small soluble and monomeric protein that performs a central step in the bioenergetic metabolism of sulfate reducing bacteria, termed "proton-thrusting," linking the oxidation of molecular hydrogen with the reduction of sulfate. The mechano-chemical coupling involved in the transfer of multiple electrons and protons in cytochrome c(3) from Desulfovibrio desulfuricans ATCC 27774 is described using results derived from the microscopic thermodynamic characterization of the redox and acid-base centers involved, crystallographic studies in the oxidized and reduced states of the cytochrome, and theoretical studies of the redox and acid-base transitions. This proton-assisted two-electron step involves very small, localized structural changes that are sufficient to generate the complex network of functional cooperativities leading to energy transduction, while using molecular mechanisms distinct from those established for other Desulfovibrio sp. cytochromes from the same structural family. PubMed: 11551953DOI: 10.1074/JBC.M107136200 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.05 Å) |
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