On the Structure and Reaction Mechanism of Human Acireductone Dioxygenase.

ABSTRACT: Acireductone dioxygenase (ARD) is an intriguing enzyme from the methionine salvage pathway that is capable of catalysing two different oxidation reactions with the same substrate depending on the type of the metal ion in the active site. To date, the structural information regarding the ARD-acireductone complex is limited and possible reaction mechanisms are still under debate. The results of joint experimental and computational studies undertaken to advance knowledge about ARD are reported. The crystal structure of an ARD from Homo sapiens was determined with selenomethionine. EPR spectroscopy suggested that binding acireductone triggers one protein residue to dissociate from Fe²⁺ , which allows NO (and presumably O₂ ) to bind directly to the metal. Mössbauer spectro

SUBMITTER: Milaczewska A 

PROVIDER: S-EPMC7883896 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature