Identification of a novel conserved sequence motif in flavoprotein hydroxylases with a putative dual function in FAD/NAD(P)H bindingMichel H. M. Eppink, Herman Schreuder, Willem J. H. van Berkel|Protein Science|1997Cited by 157
Crystal Structures of Wild-Type p-Hydroxybenzoate Hydroxylase Complexed with 4-Aminobenzoate, 2,4-Dihydroxybenzoate, and 2-Hydroxy-4-aminobenzoate and of the Tyr222Ala Mutant Complexed with 2-Hydroxy-4-aminobenzoate. Evidence for a Proton Channel and a New Binding Mode of the Flavin RingHerman Schreuder, Willem J. H. van Berkel, Andrea Mattevi et al.|Biochemistry|1994Cited by 108
Crystal structure of <i>p</i>‐hydroxybenzoate hydroxylase reconstituted with the modified fad present in alcohol oxidase from methylotrophic yeasts: Evidence for an arabinoflavinWillem J. H. van Berkel, Herman Schreuder, Michel H. M. Eppink|Protein Science|1994Cited by 60
Interdomain binding of NADPH in p-Hydroxybenzoate Hydroxylase as Suggested by Kinetic, Crystallographic and Modeling Studies of Histidine 162 and Arginine 269 VariantsMichel H. M. Eppink, Willem J. H. van Berkel, Herman Schreuder|Journal of Biological Chemistry|1998Cited by 59
Switch of coenzyme specificity of p -hydroxybenzoate hydroxylase 1 1Edited by A. R. FershtMichel H. M. Eppink, Willem J. H. van Berkel, Karin Overkamp et al.|Journal of Molecular Biology|1999Cited by 57