7ATJ

RECOMBINANT HORSERADISH PEROXIDASE C1A COMPLEX WITH CYANIDE AND FERULIC ACID

7ATJ の概要

• エントリーDOI: 10.2210/pdb7atj/pdb
• 関連するPDBエントリー: 6ATJ
• 分子名称: PEROXIDASE C1A, CALCIUM ION, CYANIDE ION, ... (6 entities in total)
• 機能のキーワード: peroxidase, oxidoreductase, cyanide, ferulic acid
• 由来する生物種: Armoracia rusticana
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35059.17

構造登録者

Henriksen, A.,Smith, A.T.,Gajhede, M. (登録日: 1999-04-26, 公開日: 2000-01-14, 最終更新日: 2024-10-16)

主引用文献

Henriksen, A.,Smith, A.T.,Gajhede, M.
The structures of the horseradish peroxidase C-ferulic acid complex and the ternary complex with cyanide suggest how peroxidases oxidize small phenolic substrates.
J.Biol.Chem., 274:35005-35011, 1999

PubMed Abstract: We have solved the x-ray structures of the binary horseradish peroxidase C-ferulic acid complex and the ternary horseradish peroxidase C-cyanide-ferulic acid complex to 2.0 and 1.45 A, respectively. Ferulic acid is a naturally occurring phenolic compound found in the plant cell wall and is an in vivo substrate for plant peroxidases. The x-ray structures demonstrate the flexibility and dynamic character of the aromatic donor binding site in horseradish peroxidase and emphasize the role of the distal arginine (Arg(38)) in both substrate oxidation and ligand binding. Arg(38) hydrogen bonds to bound cyanide, thereby contributing to the stabilization of the horseradish peroxidase-cyanide complex and suggesting that the distal arginine will be able to contribute with a similar interaction during stabilization of a bound peroxy transition state and subsequent O-O bond cleavage. The catalytic arginine is additionally engaged in an extensive hydrogen bonding network, which also includes the catalytic distal histidine, a water molecule and Pro(139), a proline residue conserved within the plant peroxidase superfamily. Based on the observed hydrogen bonding network and previous spectroscopic and kinetic work, a general mechanism of peroxidase substrate oxidation is proposed.

PubMed: 10574977
DOI: 10.1074/jbc.274.49.35005

実験手法

X-RAY DIFFRACTION (1.47 Å)