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International Journal of Molecular Sciences|February 28, 2013
Form follows function: structural and catalytic variation in the class a flavoprotein monooxygenasesKaren Crozier-Reabe, Graham R MoranMethods in Enzymology|May 11, 2019
Anaerobic methods for the transient-state study of flavoproteins: The use of specialized glassware to define the concentration of dioxygenGraham R MoranArchives of Biochemistry and Biophysics|December 8, 2004
4-Hydroxyphenylpyruvate dioxygenaseGraham R MoranBiochimica Et Biophysica Acta|April 23, 2015
The catalytic function of renalase: A decade of phantomsGraham R MoranArchives of Biochemistry and Biophysics|November 12, 2013
4-Hydroxyphenylpyruvate dioxygenase and hydroxymandelate synthase: exemplars of the α-keto acid dependent oxygenasesGraham R MoranJournal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry|April 14, 2007
The diverse and pervasive chemistries of the alpha-keto acid dependent enzymesVincent Purpero, Graham R MoranJournal of Inorganic Biochemistry|August 9, 2011
Structural and mechanistic comparisons of the metal-binding members of the vicinal oxygen chelate (VOC) superfamilyPanqing He, Graham R MoranCurrent Opinion in Chemical Biology|July 24, 2009
We two alone will sing: the two-substrate alpha-keto acid-dependent oxygenasesPanqing He, Graham R MoranBiochemistry|August 27, 2003
Interaction of (4-hydroxyphenyl)pyruvate dioxygenase with the specific inhibitor 2-[2-nitro-4-(trifluoromethyl)benzoyl]-1,3-cyclohexanedioneMichael Kavana, Graham R MoranInorganica Chimica Acta|May 23, 2008
The Interaction of Hydroxymandelate Synthase with the 4-Hydroxyphenylpyruvate Dioxygenase Inhibitor: NTBCJohn A Conrad, Graham R MoranPageof 8