High-resolution neutron crystallography visualizes an OH-bound resting state of a copper-containing nitrite reductase.

ABSTRACT: Copper-containing nitrite reductases (CuNIRs) transform nitrite to gaseous nitric oxide, which is a key process in the global nitrogen cycle. The catalytic mechanism has been extensively studied to ultimately achieve rational control of this important geobiochemical reaction. However, accumulated structural biology data show discrepancies with spectroscopic and computational studies; hence, the reaction mechanism is still controversial. In particular, the details of the proton transfer involved in it are largely unknown. This situation arises from the failure of determining positions of hydrogen atoms and protons, which play essential roles at the catalytic site of CuNIRs, even with atomic resolution X-ray crystallography. Here, we determined the 1.50 Å resolution neutron structure of a Cu

SUBMITTER: Fukuda Y 

PROVIDER: S-EPMC7049163 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature