6TAE

Neutron structure of ferric ascorbate peroxidase

6TAE の概要

• エントリーDOI: 10.2210/pdb6tae/pdb
• 分子名称: Ascorbate peroxidase, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: ascorbate peroxidase, neutron crystallography, heme peroxidase, proton pathway, 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: 29074.45

構造登録者

Kwon, H.,Basran, J.,Devos, J.M.,Schrader, T.E.,Ostermann, A.,Blakeley, M.P.,Raven, E.L.,Moody, P.C.E. (登録日: 2019-10-29, 公開日: 2020-03-18, 最終更新日: 2024-05-01)

主引用文献

Kwon, H.,Basran, J.,Devos, J.M.,Suardiaz, R.,van der Kamp, M.W.,Mulholland, A.J.,Schrader, T.E.,Ostermann, A.,Blakeley, M.P.,Moody, P.C.E.,Raven, E.L.
Visualizing the protons in a metalloenzyme electron proton transfer pathway.
Proc.Natl.Acad.Sci.USA, 117:6484-6490, 2020

PubMed Abstract: In redox metalloenzymes, the process of electron transfer often involves the concerted movement of a proton. These processes are referred to as proton-coupled electron transfer, and they underpin a wide variety of biological processes, including respiration, energy conversion, photosynthesis, and metalloenzyme catalysis. The mechanisms of proton delivery are incompletely understood, in part due to an absence of information on exact proton locations and hydrogen bonding structures in a bona fide metalloenzyme proton pathway. Here, we present a 2.1-Å neutron crystal structure of the complex formed between a redox metalloenzyme (ascorbate peroxidase) and its reducing substrate (ascorbate). In the neutron structure of the complex, the protonation states of the electron/proton donor (ascorbate) and all of the residues involved in the electron/proton transfer pathway are directly observed. This information sheds light on possible proton movements during heme-catalyzed oxygen activation, as well as on ascorbate oxidation.

PubMed: 32152099
DOI: 10.1073/pnas.1918936117

実験手法

NEUTRON DIFFRACTION (2.222 Å)
X-RAY DIFFRACTION (1.9 Å)