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1GM4

OXIDISED STRUCTURE OF CYTOCHROME C3 FROM DESULFOVIBRIO DESULFURICANS ATCC 27774 at pH 7.6

1GM4 の概要
エントリーDOI10.2210/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: 11551953
DOI: 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)
構造検証レポート
Validation report summary of 1gm4
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-11-06に公開中

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