Measuring the Orientation of Taurine in the Active Site of the Non-Heme Fe(II)/α-Ketoglutarate-Dependent Taurine Hydroxylase (TauD) Using Electron Spin Echo Envelope Modulation (ESEEM) Spectroscopy-Reference-Cited by-同舟云学术

Measuring the Orientation of Taurine in the Active Site of the Non-Heme Fe(II)/α-Ketoglutarate-Dependent Taurine Hydroxylase (TauD) Using Electron Spin Echo Envelope Modulation (ESEEM) Spectroscopy

Published:2013-08-29 Issue:36 Volume:117 Page:10384-10394
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Casey Thomas M.¹,Grzyska Piotr K.¹,Hausinger Robert P.¹,McCracken John¹

Affiliation:

1. Department of Chemistry, ‡Department of Microbiology and Molecular Genetics, and Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan, 48824

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp404743d

Reference46 articles.

1. Characterization of α-Ketoglutarate-dependent Taurine Dioxygenase from Escherichia coli

2. Fe(II)/α-Ketoglutarate-Dependent Hydroxylases and Related Enzymes

3. The diverse and pervasive chemistries of the α-keto acid dependent enzymes

4. Structural and mechanistic comparisons of the metal-binding members of the vicinal oxygen chelate (VOC) superfamily

5. FeII/α-ketoglutarate hydroxylases involved in nucleobase, nucleoside, nucleotide, and chromatin metabolism

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