1OAG

Ascorbate peroxidase from soybean cytosol

1OAG の概要

• エントリーDOI: 10.2210/pdb1oag/pdb
• 関連するPDBエントリー: 1OAF
• 分子名称: ASCORBATE PEROXIDASE, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: oxidoreductase, heme peroxidase, peroxide scavenge, ascorbate peroxidase
• 由来する生物種: GLYCINE MAX (SOYBEAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29074.45

構造登録者

Sharp, K.H.,Raven, E.L.,Moody, P.C.E. (登録日: 2003-01-13, 公開日: 2003-03-20, 最終更新日: 2023-12-13)

主引用文献

Sharp, K.H.,Mewies, M.,Moody, P.C.E.,Raven, E.L.
Crystal Structure of the Ascorbate Peroxidase-Ascorbate Complex
Nat.Struct.Biol., 10:303-, 2003

PubMed Abstract: Heme peroxidases catalyze the H2O2-dependent oxidation of a variety of substrates, most of which are organic. Mechanistically, these enzymes are well characterized: they share a common catalytic cycle that involves formation of a two-electron, oxidized Compound I intermediate followed by two single-electron reduction steps by substrate. The substrate specificity is more diverse--most peroxidases oxidize small organic substrates, but there are prominent exceptions--and there is a notable absence of structural information for a representative peroxidase-substrate complex. Thus, the features that control substrate specificity remain undefined. We present the structure of the complex of ascorbate peroxidase-ascorbate. The structure defines the ascorbate-binding interaction for the first time and provides new rationalization of the unusual functional features of the related cytochrome c peroxidase enzyme, which has been a benchmark for peroxidase catalysis for more than 20 years. A new mechanism for electron transfer is proposed that challenges existing views of substrate oxidation in other peroxidases.

PubMed: 12640445
DOI: 10.1038/NSB913

実験手法

X-RAY DIFFRACTION (1.75 Å)