XAFS of human tyrosine hydroxylase

W. Meyer*, J. Haavik, H. Winkler, A. X. Trautwein, H. F. Nolting

*Corresponding author for this work


Tyrosine hydroxylase (TH) catalyses the rate-limiting step (hydroxylation of tyrosine to form dihydroxyphenylalanine) in the biosynthetic pathway leading to the catecholamines dopamine, noradrenaline and adrenaline. The human enzyme (hTH) is present in four isoforms, generated by splicing of pre-mRNA. The purified apoenzyme (metal free) binds stoichiometric amounts of iron. The incorporation of Fe(II) results in a rapid and up to 40-fold increase of activity [1]. Besides the coordination of the metal centers in native enzyme we studied the purported inhibition of TH by its immediate products. So we analysed Fe-hTH isoform 1 native as well as oxidized with dopamine and Co-hTH isoform 2.

Original languageEnglish
JournalPhysica B: Physics of Condensed Matter
Issue numberC
Pages (from-to)717-718
Number of pages2
Publication statusPublished - 01.03.1995


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