Ultrafast Solvation Dynamics of Flavin Mononucleotide in the Reductase Component of p-Hydroxyphenylacetate Hydroxylase-Reference-Cited by-同舟云学术

Ultrafast Solvation Dynamics of Flavin Mononucleotide in the Reductase Component of p-Hydroxyphenylacetate Hydroxylase

Published:2009-06-01 Issue:25 Volume:113 Page:8439-8442
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Chosrowjan Haik¹,Taniguchi Seiji¹,Mataga Noboru¹,Phongsak Thanawat¹,Sucharitakul Jeerus¹,Chaiyen Pimchai¹,Tanaka Fumio¹

Affiliation:

1. Institute for Laser Technology, Utsubo-Hommachi 1-8-4, Nishiku, Osaka, 550-0004, Japan, Department of Biochemistry and Center for Excellence in Protein Structure and Function, Faculty of Science, Mahidol University, Bangkok 10400, Thailand, Department of Biochemistry, Faculty of Dentistry, Chulalongkorn University, Henri-Dunant Road, Patumwan, Bangkok, 10300, Thailand, SC1-413 Department of Chemistry, Faculty of Science, Mahasarakham University, Mahasarakham 44150, Thailand

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/jp901136y

Reference25 articles.

1. A novel two-protein component flavoprotein hydroxylase

2. Cloning and expression of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii: evidence of the divergence of enzymes in the class of two-protein component aromatic hydroxylases

3. The Reductase of p-Hydroxyphenylacetate 3-Hydroxylase from Acinetobacter baumannii Requires p-Hydroxyphenylacetate for Effective Catalysis

4. Kinetics of a Two-Component p-Hydroxyphenylacetate Hydroxylase Explain How Reduced Flavin Is Transferred from the Reductase to the Oxygenase

5. Kinetic Mechanisms of the Oxygenase from a Two-component Enzyme, p-Hydroxyphenylacetate 3-Hydroxylase from Acinetobacter baumannii

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