Cargando…
Characterization of the quinol-dependent nitric oxide reductase from the pathogen Neisseria meningitidis, an electrogenic enzyme
Bacterial nitric oxide reductases (NORs) catalyse the reduction of NO to N(2)O and H(2)O. 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 supe...
Autores principales: | Gonska, Nathalie, Young, David, Yuki, Riki, Okamoto, Takuya, Hisano, Tamao, Antonyuk, Svetlana, Hasnain, S. Samar, Muramoto, Kazumasa, Shiro, Yoshitsugu, Tosha, Takehiko, Ädelroth, Pia |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5826923/ https://www.ncbi.nlm.nih.gov/pubmed/29483528 http://dx.doi.org/10.1038/s41598-018-21804-0 |
Ejemplares similares
-
The active form of quinol-dependent nitric oxide reductase from Neisseria meningitidis is a dimer
por: Jamali, M. Arif M., et al.
Publicado: (2020) -
Dimeric structures of quinol-dependent nitric oxide reductases (qNORs) revealed by cryo–electron microscopy
por: Gopalasingam, Chai C., et al.
Publicado: (2019) -
A 2.2 Å cryoEM structure of a quinol-dependent NO Reductase shows close similarity to respiratory oxidases
por: Flynn, Alex J., et al.
Publicado: (2023) -
Structural basis for heme detoxification by an ATP-binding cassette–type efflux pump in gram-positive pathogenic bacteria
por: Nakamura, Hiro, et al.
Publicado: (2022) -
An unprecedented dioxygen species revealed by serial femtosecond rotation crystallography in copper nitrite reductase
por: Halsted, Thomas P., et al.
Publicado: (2018)