Year: 1998
Type: article
Abstract: Tyrosine 196 in Old Yellow Enzyme (OYE) was mutated to phenylalanine, and the resulting mutant enzyme was characterized to evaluate the mechanistic role of the residue. The residue demonstrates little effect on ligand binding and the reductive half-reaction, but a dramatic slowing by nearly 6 orders of magnitude of its oxidative half-reaction with 2-cyclohexenone. Observation of the oxidative half-reaction with a series of substrates allows us to propose a model describing the mechanism of the oxidative half-reaction. In addition, the curtailed reactivity with enones allows for characterization of the manner in which reduced enzyme primes the substrate for the redox reaction by observation of the Michaelis complex with reduced enzyme bound to substrate.
Source: Journal of Biological Chemistry
Authors: Rahul M. Kohli, Vincent Massey
Institution: University of Michigan
Language: English
Subfield: Inorganic Chemistry
Field: Chemistry
Domain: Physical Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
Award: G2869093499
OpenAlex ID: W2001382343