6ZUB

Cu nitrite reductase from Achromobacter cycloclastes: MSOX series at 170K, dose point 2

6ZUB の概要

• エントリーDOI: 10.2210/pdb6zub/pdb
• 分子名称: Copper-containing nitrite reductase, COPPER (II) ION, NITRITE ION, ... (6 entities in total)
• 機能のキーワード: cu nitrite reductase, nitrosyl, copper, msox, oxidoreductase
• 由来する生物種: Achromobacter cycloclastes
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37134.61

構造登録者

Hough, M.A.,Antonyuk, S.V.,Strange, R.W.,Hasnain, S.S. (登録日: 2020-07-22, 公開日: 2021-06-23, 最終更新日: 2024-01-31)

主引用文献

Hough, M.A.,Conradie, J.,Strange, R.W.,Antonyuk, S.V.,Eady, R.R.,Ghosh, A.,Hasnain, S.S.
Nature of the copper-nitrosyl intermediates of copper nitrite reductases during catalysis.
Chem Sci, 11:12485-12492, 2020

PubMed Abstract: The design and synthesis of copper complexes that can reduce nitrite to NO has attracted considerable interest. They have been guided by the structural information on the catalytic Cu centre of the widespread enzymes Cu nitrite reductases but the chemically novel side-on binding of NO observed in all crystallographic studies of these enzymes has been questioned in terms of its functional relevance. We show conversion of NO to NO in the crystal maintained at 170 K and present 'molecular movies' defining events during enzyme turnover including the formation of side-on Cu-NO intermediate. DFT modelling suggests that both {CuNO} and {CuNO} states may occur as side-on forms in an enzymatic active site with the stability of the {CuNO} side-on form governed by the protonation state of the histidine ligands. Formation of a copper-nitrosyl intermediate thus needs to be accommodated in future design templates for functional synthetic Cu-NiR complexes.

PubMed: 34094452
DOI: 10.1039/d0sc04797j

実験手法

X-RAY DIFFRACTION (1.08 Å)