Citation: P. Sobrado et al., Probing the relative timing of hydrogen abstraction steps in the flavocytochrome b(2) reaction with primary and solvent deuterium isotope effects andmutant enzymes, BIOCHEM, 40(4), 2001, pp. 994-1001
Authors:
McCulloch, RI
Daubner, SC
Fitzpatrick, PF
Citation: Ri. Mcculloch et al., Effects of substitution at serine 40 of tyrosine hydroxylase on catecholamine binding, BIOCHEM, 40(24), 2001, pp. 7273-7278
Citation: Sc. Daubner et al., Reversing the substrate specificities of phenylalanine and tyrosine hydroxylase: Aspartate 425 of tyrosine hydroxylase is essential for L-DOPA formation, BIOCHEM, 39(32), 2000, pp. 9652-9661
Citation: Hr. Ellis et al., Mutation of serine 395 of tyrosine hydroxylase decouples oxygen-oxygen bond cleavage and tyrosine hydroxylation, BIOCHEM, 39(14), 2000, pp. 4174-4181
Authors:
Ellis, HR
Daubner, SC
McCulloch, RI
Fitzpatrick, PF
Citation: Hr. Ellis et al., Phenylalanine residues in the active site of tyrosine hydroxylase: Mutagenesis of Phe300 and Phe309 to alanine and metal ion-catalyzed hydroxylation of Phe300, BIOCHEM, 38(34), 1999, pp. 10909-10914
Citation: Sc. Daubner et Pf. Fitzpatrick, Site-directed mutants of charged residues in the active site of tyrosine hydroxylase, BIOCHEM, 38(14), 1999, pp. 4448-4454