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JBIC Journal of Biological Inorganic Chemistry : Volume 4, Issue 1, February 1999

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Iron coordination geometry in full-length, truncated, and dehydrated forms of human tyrosine hydroxylase studied by Mössbauer and X-ray absorption spectroscopy

Content Provider	Springer Nature Link
Author	Schünemann, Volker Meier, Christian Meyer Klaucke, Wolfram Winkler, Heiner Trautwein, Alfred X. Knappskog, Per M. Toska, Karen Haavik, J.
Copyright Year	1999
Abstract	Full-length human tyrosine hydroxylase 1 (hTH1) and a truncated enzyme lacking the 150 N-terminal amino acids were expressed in Escherichia coli and purified either with or without (6×histidine) N-terminal tags. After reconstitution with 57Fe(II), the Mössbauer and X-ray absorption spectra of the enzymes were compared before and after dehydration by lyophilization. Before dehydration, >90% of the iron in hTH1 had Mössbauer parameters typical for high-spin Fe(II) in a six-coordinate environment [isomer shift δ(1.8–77 K)=1.26–1.24 mm s–1 and quadrupole splitting ΔE Q=2.68 mm s–1]. After dehydration, the Mössbauer spectrum changed and 63% of the area could be attributed to five-coordinate high-spin Fe(II) (δ=1.07 mm s–1 and ΔE Q=2.89 mm s–1 at 77 K), whereas 28% of the iron remained as six-coordinate high-spin Fe(II) (δ=1.24 mm s–1 and ΔE Q=2.87 mm s–1 at 77 K). Similar changes upon dehydration were observed for truncated TH either with or without the histidine tag. After rehydration of hTH1 the spectroscopic changes were completely reversed. The X-ray absorption spectra of hTH1 in solution and in lyophilized form, and for the truncated protein in solution, corroborate the findings derived from the Mössbauer spectra. The pre-edge peak intensity of the protein in solution indicates six-coordination of the iron, while that of the dehydrated protein is typical for a five-coordinate iron center. Thus, the active-site iron can exist in different coordination states, which can be interconverted depending on the hydration state of the protein, indicating the presence or absence of a water molecule as a coordinating ligand to the iron. The present study explains the difference in iron coordination determined by X-ray crystallography, which has shown a five-coordinate iron center in rat TH, and by our recent spectroscopic study of human TH in solution, which showed a six-coordinated iron center.
Starting Page	223
Ending Page	231
Page Count	9
File Format	PDF
ISSN	09498257
Journal	JBIC Journal of Biological Inorganic Chemistry
Volume Number	4
Issue Number	2
e-ISSN	14321327
Language	English
Publisher	Springer-Verlag
Publisher Date	1999-05-05
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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