Metal Coordination Environment of a Cu(II)-Substituted α-Keto Acid-Dependent Dioxygenase That Degrades the Herbicide 2,4-D-Reference-Cited by-同舟云学术

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Metal Coordination Environment of a Cu(II)-Substituted α-Keto Acid-Dependent Dioxygenase That Degrades the Herbicide 2,4-D

Published:1997-04-01 Issue:14 Volume:119 Page:3413-3414
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Whiting Adam K.,Que Lawrence,Saari Ruth E.,Hausinger Robert P.,Fredrick Matthew A.,McCracken John

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja964449x

Reference19 articles.

1. Alcaligenes eutrophus JMP134 "2,4-dichlorophenoxyacetate monooxygenase" is an alpha-ketoglutarate-dependent dioxygenase

2. Purification and characterization of 2,4-dichlorophenoxyacetate/alpha-ketoglutarate dioxygenase.

3. Structural implications derived from the analysis of electron paramagnetic resonance spectra of natural and artificial copper proteins

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1. Characterization of Cu(II)-reconstituted ACC Oxidase using experimental and theoretical approaches;Archives of Biochemistry and Biophysics;2017-06

2. Substrate Positioning by Gln239 Stimulates Turnover in Factor Inhibiting HIF, an αKG-Dependent Hydroxylase;Biochemistry;2014-08-29

3. Structural Insight into the Prolyl Hydroxylase PHD2: A Molecular Dynamics and DFT Study;European Journal of Inorganic Chemistry;2012-08-29

4. Screening chelating inhibitors of HIF-prolyl hydroxylase domain 2 (PHD2) and factor inhibiting HIF (FIH);Journal of Inorganic Biochemistry;2012-08

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