A QM/MM Study of Nitrite Binding Modes in a Three-Domain Heme-Cu Nitrite Reductase.

ABSTRACT: Copper-containing nitrite reductases (CuNiRs) play a key role in the global nitrogen cycle by reducing nitrite (NO₂^-) to nitric oxide, a reaction that involves one electron and two protons. In typical two-domain CuNiRs, the electron is acquired from an external electron-donating partner. The recently characterised Rastonia picketti (RpNiR) system is a three-domain CuNiR, where the cupredoxin domain is tethered to a heme c domain that can function as the electron donor. The nitrite reduction starts with the binding of NO₂^- to the T2Cu centre, but very little is known about how NO₂^- binds to native RpNiR. A recent crystallographic study of an RpNiR mutant suggests that NO₂^- may bind via nitrogen rather than throug

SUBMITTER: Sen K 

PROVIDER: S-EPMC6278305 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature