6FWF

Low resolution structure of Neisseria meningitidis qNOR

「6ELH」から置き換えられました

6FWF の概要

• エントリーDOI: 10.2210/pdb6fwf/pdb
• 関連するPDBエントリー: 6ELH
• 分子名称: Nitric-oxide reductase, PROTOPORPHYRIN IX CONTAINING FE, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: reductase, membrane-bound, nitric oxide, oxidoreductase
• 由来する生物種: Neisseria meningitidis (strain alpha14)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 85718.11

構造登録者

Young, D.,Antonyuk, S.,Tosha, T.,Hisano, T.,Hasnain, S.,Shiro, Y. (登録日: 2018-03-06, 公開日: 2018-03-14, 最終更新日: 2024-01-17)

主引用文献

Gonska, N.,Young, D.,Yuki, R.,Okamoto, T.,Hisano, T.,Antonyuk, S.,Hasnain, S.S.,Muramoto, K.,Shiro, Y.,Tosha, T.,Adelroth, P.
Characterization of the quinol-dependent nitric oxide reductase from the pathogen Neisseria meningitidis, an electrogenic enzyme.
Sci Rep, 8:3637-, 2018

PubMed Abstract: Bacterial nitric oxide reductases (NORs) catalyse the reduction of NO to NO and HO. NORs are found either in denitrification chains, or in pathogens where their primary role is detoxification of NO produced by the immune defense of the host. Although NORs belong to the heme-copper oxidase superfamily, comprising proton-pumping O-reducing enzymes, the best studied NORs, cNORs (cytochrome c-dependent), are non-electrogenic. Here, we focus on another type of NOR, qNOR (quinol-dependent). Recombinant qNOR from Neisseria meningitidis, a human pathogen, purified from Escherichia coli, showed high catalytic activity and spectroscopic properties largely similar to cNORs. However, in contrast to cNOR, liposome-reconstituted qNOR showed respiratory control ratios above two, indicating that NO reduction by qNOR was electrogenic. Further, we determined a 4.5 Å crystal structure of the N. meningitidis qNOR, allowing exploration of a potential proton transfer pathway from the cytoplasm by mutagenesis. Most mutations had little effect on the activity, however the E-498 variants were largely inactive, while the corresponding substitution in cNOR was previously shown not to induce significant effects. We thus suggest that, contrary to cNOR, the N. meningitidis qNOR uses cytoplasmic protons for NO reduction. Our results allow possible routes for protons to be discussed.

PubMed: 29483528
DOI: 10.1038/s41598-018-21804-0

実験手法

X-RAY DIFFRACTION (4.2 Å)