Origin of Catalysis by Nitroalkane Oxidase.

ABSTRACT: The rate of proton abstraction of the carbon acid nitroethane by Asp402 is accelerated by a factor of 10⁸ in the enzyme nitroalkane oxidase (NAO) relative to that by the organic base acetate ion in water. The Cα proton of nitroalkanes is known to exhibit an abnormal correlation between its acidity strength and the rate of deprotonation, with an unusually slow rate of deprotonation in water. This work examines the origin of NAO catalysis, revealing that the rate enhancement by the enzyme is due to transition-state stabilization, restoring the normal behavior of the linear free energy relationship of Bronsted acids. Interestingly, NAO employs the ubiquitous cofactor flavin adenosine diphosphate (FAD) to perform the subsequent oxidation. Does the FAD cofactor also affect the cataly

SUBMITTER: Major DT 

PROVIDER: S-EPMC12753276 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature