Computational studies of electron-transfer processes in old yellow enzyme
Document Type
Conference Proceeding
Publication Date
12-20-2001
Department
Department of Chemistry; Department of Biological Sciences
Abstract
Old Yellow Enzyme (OYE) is a flavoenzyme that was first isolated from brewer's bottom yeast. Homologues have been identified in other strains of yeast, bacteria, and plants. In plants, the OYE homologue functions enzymatically in the synthesis of plant hormones, but the biological function of OYE in yeast is still unknown. Flavin mononucleotide (FMN) is the cofactor that is noncovalently bound in the enzyme. OYE binds several phenolic ligands that serve as models for reactive biological substrates. These complexes have broad long-wavelength absorption bands, which have been ascribed to charge-transfer interactions, with the phenolate anion acting as the electron donor and the FMN as the acceptor [Abramovitz, A. S.; Massey, V. J Bio Chem 1976, 251, 5327-5336]. The computational characterization of these electronic transitions in the active site will help in understanding the biological processes in the enzyme. It was found that at several levels of computational methods, and through computationally mutating relevant amino acids, a charge-transfer process is occurring. This result agrees with previous experimental work and is consistent with all ultraviolet-visible spectrophotometric data. The preliminary results for the computational studies of these electron-transfer processes will be presented.
Publication Title
International Journal of Quantum Chemistry
Recommended Citation
Chateauneuf, G. M.,
Brown, R.,
&
Brown, B.
(2001).
Computational studies of electron-transfer processes in old yellow enzyme.
International Journal of Quantum Chemistry,
85(6), 685-692.
http://doi.org/10.1002/qua.1118
Retrieved from: https://digitalcommons.mtu.edu/michigantech-p/3888