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International Journal of Molecular Sciences|December 4, 2012
Noncanonical reactions of flavoenzymesPablo SobradoArchives of Biochemistry and Biophysics|November 27, 2020
Role of reduced flavin in dehalogenation reactionsPablo SobradoMethods in Enzymology|May 11, 2019
Performing anaerobic stopped-flow spectrophotometry inside of an anaerobic chamberHannah Valentino, Pablo SobradoBiochemistry|September 13, 2021
Characterization of a Nitro-Forming Enzyme Involved in Fosfazinomycin BiosynthesisHannah Valentino, Pablo SobradoMolecules (Basel, Switzerland)|October 5, 2017
Characterization of the Ornithine Hydroxylation Step in Albachelin BiosynthesisKendra Bufkin, Pablo SobradoBiochemistry|August 30, 2011
Substrate binding modulates the activity of Mycobacterium smegmatis G, a flavin-dependent monooxygenase involved in the biosynthesis of hydroxamate-containing siderophoresReeder Robinson, Pablo SobradoBiochemistry|June 7, 2018
Kinetic Solvent Viscosity Effects as Probes for Studying the Mechanisms of Enzyme ActionGiovanni Gadda, Pablo SobradoBiochemistry|November 26, 2003
Analysis of the role of the active site residue Arg98 in the flavoprotein tryptophan 2-monooxygenase, a member of the L-amino oxidase familyPablo Sobrado, Paul F FitzpatrickBiochemistry|November 26, 2003
Identification of Tyr413 as an active site residue in the flavoprotein tryptophan 2-monooxygenase and analysis of its contribution to catalysisPablo Sobrado, Paul F FitzpatrickBiochemistry|July 10, 2010
Aspergillus fumigatus SidA is a highly specific ornithine hydroxylase with bound flavin cofactorSamuel W Chocklett, Pablo SobradoPageof 9