Spectroscopy and Kinetics of Wild-Type and Mutant Tyrosine Hydroxylase: Mechanistic Insight into O2 Activation-Reference-Cited by-同舟云学术

Spectroscopy and Kinetics of Wild-Type and Mutant Tyrosine Hydroxylase: Mechanistic Insight into O2 Activation

Published:2009-05-12 Issue:22 Volume:131 Page:7685-7698
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Chow Marina S.¹,Eser Bekir E.¹,Wilson Samuel A.¹,Hodgson Keith O.¹,Hedman Britt¹,Fitzpatrick Paul F.¹,Solomon Edward I.¹

Affiliation:

1. Department of Chemistry, Stanford University, Stanford, California 94305, Stanford Synchrotron Radiation Lightsource, SLAC, Stanford University, Stanford, California 94309, and Department of Biochemistry and Biophysics and Department of Chemistry, Texas A&M University, College Station, Texas 77843

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja810080c

Reference70 articles.

1. Tetrahydropterin-Dependent Amino Acid Hydroxylases

2. Structure and function of the aromatic amino acid hydroxylases

3. Pterin-Dependent Amino Acid Hydroxylases

4. Recessively inherited L-DOPA-responsive parkinsonism in infancy caused by a point mutation (L205P) in the tyrosine hydroxylase gene

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