6V59

Crystal structure of the diheme peroxidase BthA Y463M variant from Burkholderia thailandensis E264

6V59 の概要

• エントリーDOI: 10.2210/pdb6v59/pdb
• 分子名称: Di-haem cytochrome c peroxidase family protein, HEME C, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: heme, peroxidase, diheme, oxidoreductase, btha
• 由来する生物種: Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 106260.54

構造登録者

Cohen, S.E.,Drennan, C.L. (登録日: 2019-12-03, 公開日: 2020-07-08, 最終更新日: 2024-10-30)

主引用文献

Rizzolo, K.,Weitz, A.C.,Cohen, S.E.,Drennan, C.L.,Hendrich, M.P.,Elliott, S.J.
A Stable Ferryl Porphyrin at the Active Site of Y463M BthA.
J.Am.Chem.Soc., 142:11978-11982, 2020

PubMed Abstract: BthA is a diheme enzyme that is a member of the bacterial cytochrome c peroxidase superfamily, capable of generating a highly unusual Fe(IV)Fe(IV)═O oxidation state, known to be responsible for long-range oxidative chemistry in the enzyme MauG. Here, we show that installing a canonical Met ligand in lieu of the Tyr found at the heme of MauG associated with electron transfer, results in a construct that yields an unusually stable Fe(IV)═O porphyrin at the peroxidatic heme. This state is spontaneously formed at ambient conditions using either molecular O or HO. The resulting data illustrate how a ferryl iron, with unforeseen stability, may be achieved in biology.

PubMed: 32564595
DOI: 10.1021/jacs.0c04023

実験手法

X-RAY DIFFRACTION (1.593 Å)