2BLF

Sulfite dehydrogenase from Starkeya Novella

2BLF の概要

• エントリーDOI: 10.2210/pdb2blf/pdb
• 関連するPDBエントリー: 2BPB
• 分子名称: Sulfite:cytochrome c oxidoreductase subunit A, Sulfite:cytochrome c oxidoreductase subunit B, (MOLYBDOPTERIN-S,S)-OXO-MOLYBDENUM, ... (6 entities in total)
• 機能のキーワード: sulfite oxidase, molybdopterin, c-type cytochrome, heme, electron transport, oxidoreductase
• 由来する生物種: Starkeya novella (Thiobacillus novellus); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 50259.39

構造登録者

Bailey, S.,Kappler, U. (登録日: 2005-03-04, 公開日: 2005-04-28, 最終更新日: 2024-11-20)

主引用文献

Kappler, U.,Bailey, S.
Molecular Basis of Intramolecular Electron Transfer in Sulfite-Oxidizing Enzymes is Revealed by High Resolution Structure of a Heterodimeric Complex of the Catalytic Molybdopterin Subunit and a C-Type Cytochrome Subunit.
J.Biol.Chem., 280:24999-, 2005

PubMed Abstract: Sulfite-oxidizing molybdoenzymes convert the highly reactive and therefore toxic sulfite to sulfate and have been identified in insects, animals, plants, and bacteria. Although the well studied enzymes from higher animals serve to detoxify sulfite that arises from the catabolism of sulfur-containing amino acids, the bacterial enzymes have a central role in converting sulfite formed during dissimilatory oxidation of reduced sulfur compounds. Here we describe the structure of the Starkeya novella sulfite dehydrogenase, a heterodimeric complex of the catalytic molybdopterin subunit and a c-type cytochrome subunit, that reveals the molecular mechanism of intramolecular electron transfer in sulfite-oxidizing enzymes. The close approach of the two redox centers in the protein complex (Mo-Fe distance 16.6 A) allows for rapid electron transfer via tunnelling or aided by the protein environment. The high resolution structure of the complex has allowed the identification of potential through-bond pathways for electron transfer including a direct link via Arg-55A and/or an aromatic-mediated pathway. A potential site of electron transfer to an external acceptor cytochrome c was also identified on the SorB subunit on the opposite side to the interaction with the catalytic SorA subunit.

PubMed: 15863498
DOI: 10.1074/JBC.M503237200

実験手法

X-RAY DIFFRACTION (1.8 Å)