T
Tai Man Louie
Researcher at Washington State University
Publications - 5
Citations - 1081
Tai Man Louie is an academic researcher from Washington State University. The author has contributed to research in topics: Flavin adenine dinucleotide & Cofactor. The author has an hindex of 5, co-authored 5 publications receiving 1031 citations. Previous affiliations of Tai Man Louie include Harvard University & Polytechnic University of Milan.
Papers
More filters
Journal ArticleDOI
Protein Conformational Dynamics Probed by Single-Molecule Electron Transfer
Haw Yang,Haw Yang,Haw Yang,Guobin Luo,Guobin Luo,Guobin Luo,Pallop Karnchanaphanurach,Pallop Karnchanaphanurach,Pallop Karnchanaphanurach,Tai Man Louie,Tai Man Louie,Tai Man Louie,Ivan Rech,Ivan Rech,Ivan Rech,Sergio Cova,Sergio Cova,Sergio Cova,Luying Xun,Luying Xun,Luying Xun,X. Sunney Xie,X. Sunney Xie,X. Sunney Xie +23 more
TL;DR: By probing the fluorescence lifetime of the single flavin on a photon-by-photon basis, the variation of flavin-tyrosine distance over time is observed, suggesting the existence of multiple interconverting conformers related to the fluctuating catalytic reactivity.
Journal ArticleDOI
Genetic and Biochemical Characterization of a 2,4,6-Trichlorophenol Degradation Pathway in Ralstonia eutropha JMP134
TL;DR: The data suggest that JMP134 transforms 2,4,6-TCP to 2-chloromaleylacetate by TcpA and TcpC, and suggests that tcpB may function as an FAD reductase, but experimental data did not support this hypothesis.
Journal ArticleDOI
Coordinated production and utilization of FADH2 by NAD(P)H-flavin oxidoreductase and 4-hydroxyphenylacetate 3-monooxygenase.
TL;DR: HpaB's high intracellular concentration, its high affinity for FADH(2), its property of protecting bound FADh(2) in the absence of 4HPA, and its ability to rapidly use F ADH( 2) to oxidize 4H PA when4HPA is available can coordinate FAD h2O production and utilization by HpaB and HpaC in vivo.
Journal ArticleDOI
FAD is a preferred substrate and an inhibitor of Escherichia coli general NAD(P)H:flavin oxidoreductase.
TL;DR: The data suggest that FAD is a preferred substrate and an inhibitor, suppressing the activities of Fre at low NADH concentrations, and the overlapping binding sites of FAD and NAD(P)H offers a plausible explanation for the largeK m values of Fre for NADH and NADPH when F AD is the electron acceptor.
Journal ArticleDOI
Identification, Purification, and Characterization of Iminodiacetate Oxidase from the EDTA-Degrading Bacterium BNC1
TL;DR: IDA oxidase is likely the second enzyme in both NTA and EDTA degradation pathways in strain BNC1, and has essentially the same enzymatic activity and properties as the native IDA oxidase.