B.J. Brown
University of Michigan
5 Papers
186 Citations
B.J. Brown is an academic researcher from University of Michigan. The author has contributed to research in topics: Enzyme & Asparagine. The author has an hindex of 4, co-authored 5 publications.
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Papers
On the active site of Old Yellow Enzyme. Role of histidine 191 and asparagine 194.
TL;DR: In this paper, Fox et al. used the crystal structure of OYE1 from brewer's bottom yeast to identify histidine 191 and asparagine 194 as amino acid residues that hydrogen-bond with the phenolic ligands, stabilizing the anionic form involved in charge-transfer interaction with the FMN prosthetic group.
145
Old yellow enzyme: Reduction of nitrate esters, glycerin trinitrate, and propylene 1,2-dinitrate
TL;DR: Analysis of the products reveal that with the enzyme-catalyzed reactions, reduction of the primary nitrate in both GTN and propylene dinitrate is favored by comparison with the free-flavin reactions, implying that the chemical mechanism of the reaction is one involving radical transfers.
53
Computational studies of electron-transfer processes in old yellow enzyme
TL;DR: It was found that at several levels of computational methods, and through computationally mutating relevant amino acids, a charge-transfer process is occurring, which agrees with previous experimental work and is consistent with all ultraviolet–visible spectrophotometric data.
4
The Role of Glutamine 114 in Old Yellow Enzyme
TL;DR: The Q114N mutation results in little change in the protein structure, moving the amide group of residue 114 out of H-bonding distance, allowing repositioning of the FMN prosthetic group to form new interactions that replace the lost H- bonding distance.
A New Old Yellow Enzyme of Saccharomyces cerevisiae
TL;DR: Although the two enzymes are clearly closely related, they show differences in ligand binding properties and in their catalytic activities with oxygen and cyclohexen-2-one as acceptors.