1E85

Cytochrome c' from Alcaligenes xylosoxidans - reduced structure with NO bound to proximal side of heme

1E85 の概要

• エントリーDOI: 10.2210/pdb1e85/pdb
• 関連するPDBエントリー: 1CGO 1E83 1E84 1E86
• 分子名称: CYTOCHROME C', HEME C, NITRIC OXIDE, ... (4 entities in total)
• 機能のキーワード: electron transport, cytochrome, heme, 4-helix bundle, nitric oxide
• 由来する生物種: ACHROMOBACTER XYLOSOXIDANS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14279.95

構造登録者

Lawson, D.M.,Stevenson, C.E.M.,Andrew, C.R.,Eady, R.R. (登録日: 2000-09-15, 公開日: 2000-11-06, 最終更新日: 2024-10-23)

主引用文献

Lawson, D.M.,Stevenson, C.E.M.,Andrew, C.R.,Eady, R.R.
Unprecedented Proximal Binding of Nitric Oxide to Heme: Implications for Guanylate Cyclase.
Embo J., 19:5661-, 2000

PubMed Abstract: Microbial cytochromes c' contain a 5-coordinate His-ligated heme that forms stable adducts with nitric oxide (NO) and carbon monoxide (CO), but not with dioxygen. We report the 1.95 and 1.35 A resolution crystal structures of the CO- and NO-bound forms of the reduced protein from Alcaligenes xylosoxidans. NO disrupts the His-Fe bond and binds in a novel mode to the proximal face of the heme, giving a 5-coordinate species. In contrast, CO binds 6-coordinate on the distal side. A second CO molecule, not bound to the heme, is located in the proximal pocket. Since the unusual spectroscopic properties of cytochromes c' are shared by soluble guanylate cyclase (sGC), our findings have potential implications for the activation of sGC induced by the binding of NO or CO to the heme domain.

PubMed: 11060017
DOI: 10.1093/EMBOJ/19.21.5661

実験手法

X-RAY DIFFRACTION (1.35 Å)