2XIH

The structure of ascorbate peroxidase Compound III

2XIH の概要

• エントリーDOI: 10.2210/pdb2xih/pdb
• 関連するPDBエントリー: 1OAF 1OAG 1V0H 2CL4 2GGN 2GHC 2GHD 2GHE 2GHH 2GHK 2VCF 2VCN 2VCS 2VNX 2VNZ 2VO2 2WD4 2XI6 2XIF
• 分子名称: ASCORBATE PEROXIDASE, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: ferryl ion, ferrous heme, oxidoreductase
• 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: 27740.02

構造登録者

Gumiero, A.,Raven, E.L.,Moody, P.C.E. (登録日: 2010-06-29, 公開日: 2010-07-07, 最終更新日: 2023-12-20)

主引用文献

Gumiero, A.,Metcalfe, C.L.,Pearson, A.R.,Raven, E.L.,Moody, P.C.
Nature of the ferryl heme in compounds I and II.
J. Biol. Chem., 286:1260-1268, 2011

PubMed Abstract: Heme enzymes are ubiquitous in biology and catalyze a vast array of biological redox processes. The formation of high valent ferryl intermediates of the heme iron (known as Compounds I and Compound II) is implicated for a number of catalytic heme enzymes, but these species are formed only transiently and thus have proved somewhat elusive. In consequence, there has been conflicting evidence as to the nature of these ferryl intermediates in a number of different heme enzymes, in particular the precise nature of the bond between the heme iron and the bound oxygen atom. In this work, we present high resolution crystal structures of both Compound I and Compound II intermediates in two different heme peroxidase enzymes, cytochrome c peroxidase and ascorbate peroxidase, allowing direct and accurate comparison of the bonding interactions in the different intermediates. A consistent picture emerges across all structures, showing lengthening of the ferryl oxygen bond (and presumed protonation) on reduction of Compound I to Compound II. These data clarify long standing inconsistencies on the nature of the ferryl heme species in these intermediates.

PubMed: 21062738
DOI: 10.1074/jbc.M110.183483

実験手法

X-RAY DIFFRACTION (1.65 Å)