4CVJ

Neutron Structure of Compound I intermediate of Cytochrome c Peroxidase - Deuterium exchanged 100 K

4CVJ の概要

• エントリーDOI: 10.2210/pdb4cvj/pdb
• 関連するPDBエントリー: 4CVI
• 分子名称: CYTOCHROME C PEROXIDASE, MITOCHONDRIAL, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: oxidoreductase, heme peroxidase, redox, electron transport, ferric, heme, protonation, enzyme intermediate
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34249.89

構造登録者

Casadei, C.M.,Gumiero, A.,Blakeley, M.P.,Ostermann, A.,Raven, E.L.,Moody, P.C.E. (登録日: 2014-03-27, 公開日: 2014-07-16, 最終更新日: 2024-05-08)

主引用文献

Casadei, C.M.,Gumiero, A.,Metcalfe, C.L.,Murphy, E.J.,Basran, J.,Concilio, M.G.,Teixeira, S.C.M.,Schrader, T.E.,Fielding, A.J.,Ostermann, A.,Blakeley, M.P.,Raven, E.L.,Moody, P.C.E.
Neutron Cryo-Crystallography Captures the Protonation State of Ferryl Heme in a Peroxidase
Science, 345:193-, 2014

PubMed Abstract: Heme enzymes activate oxygen through formation of transient iron-oxo (ferryl) intermediates of the heme iron. A long-standing question has been the nature of the iron-oxygen bond and, in particular, the protonation state. We present neutron structures of the ferric derivative of cytochrome c peroxidase and its ferryl intermediate; these allow direct visualization of protonation states. We demonstrate that the ferryl heme is an Fe(IV)=O species and is not protonated. Comparison of the structures shows that the distal histidine becomes protonated on formation of the ferryl intermediate, which has implications for the understanding of O-O bond cleavage in heme enzymes. The structures highlight the advantages of neutron cryo-crystallography in probing reaction mechanisms and visualizing protonation states in enzyme intermediates.

PubMed: 25013070
DOI: 10.1126/SCIENCE.1254398

実験手法

NEUTRON DIFFRACTION (2.501 Å)
X-RAY DIFFRACTION (2.182 Å)