Resonance Raman Studies of Catecholate and Phenolate Complexes of Recombinant Human Tyrosine Hydroxylase

• Published in: Biochemistry (Easton) Vol. 34; no. 16; pp. 5504 - 5510
• Main Authors: Michaud-Soret, Isabelle, Andersson, Kristoffer K, Que, Lawrence, Haavik, Jan
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 25.04.1995
• Subjects: Adrenal Gland Neoplasms; Adrenal Gland Neoplasms - enzymology; Adrenal Glands; Adrenal Glands - enzymology; Animals; Apoenzymes; Apoenzymes - chemistry; Apoenzymes - isolation & purification; Apoenzymes - metabolism; Binding Sites; Biochemistry; Biochemistry, Molecular Biology; Catechols; Catechols - metabolism; Cattle; Chlorides; Dopamine; Dopamine - metabolism; Escherichia coli; Ferric Compounds; Ferric Compounds - metabolism; Humans; Iron; Iron - metabolism; Isoenzymes; Isoenzymes - chemistry; Isoenzymes - isolation & purification; Isoenzymes - metabolism; Life Sciences; Norepinephrine; Norepinephrine - metabolism; Oxygen Isotopes; Pheochromocytoma; Pheochromocytoma - enzymology; Phosphorylation; Protein Conformation; Rats; Recombinant Proteins; Recombinant Proteins - chemistry; Recombinant Proteins - isolation & purification; Recombinant Proteins - metabolism; Spectrophotometry; Tyramine; Tyramine - metabolism; Tyrosine 3-Monooxygenase; Tyrosine 3-Monooxygenase - chemistry; Tyrosine 3-Monooxygenase - isolation & purification; Tyrosine 3-Monooxygenase - metabolism

Human tyrosine hydroxylase isoform 1 (hTH1) was expressed in Escherichia coli, purified as the apoenzyme, and reconstituted with iron. The resonance Raman spectra of hTH1 complexed with dopamine, noradrenaline, tyramine, and catechol have been studied and compared to those obtained for TH isolated f...