Catalytically important damage-free structures of a copper nitrite reductase obtained by femtosecond X-ray laser and room-temperature neutron crystallography.

ABSTRACT: Copper-containing nitrite reductases (CuNiRs) that convert NO₂ ^- to NO via a Cu_CAT-His-Cys-Cu_ET proton-coupled redox system are of central importance in nitrogen-based energy metabolism. These metalloenzymes, like all redox enzymes, are very susceptible to radiation damage from the intense synchrotron-radiation X-rays that are used to obtain structures at high resolution. Understanding the chemistry that underpins the enzyme mechanisms in these systems requires resolutions of better than 2 Å. Here, for the first time, the damage-free structure of the resting state of one of the most studied CuNiRs was obtained by combining X-ray free-electron laser (XFEL) and neutron crystallography. This represents the first direct comparison of neutron and XFEL

SUBMITTER: Halsted TP 

PROVIDER: S-EPMC6608623 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature