Molecular mechanism of a large conformational change of the quinone cofactor in the semiquinone intermediate of bacterial copper amine oxidase
Mitsuo Shoji, T. Murakawa, Shota Nakanishi, Mauro Boero, Yasuteru Shigeta, Hideyuki Hayashi, Toshihide Okajima
Abstract
, suggesting that the semiquinone form is catalytically active for the subsequent oxidative half-reaction in AGAO. The ingenious molecular mechanism exerted by TPQ to achieve the "state-specific" reaction sheds new light on a drastic environmental transformation around the catalytic center.
Topics & Concepts
SemiquinoneQuinoneChemistryCofactorCopperMechanism (biology)Amine oxidaseConformational changeAmine gas treatingAmine oxidase (copper-containing)StereochemistryPhotochemistryBiochemistryEnzymeOrganic chemistryDiamine oxidaseEpistemologyPhilosophyMicrobial metabolism and enzyme functionPorphyrin Metabolism and DisordersBiochemical Acid Research Studies