Vanadate-Containing Haloperoxidases and Acid Phosphatases: The Conserved Active Site
Author:
Affiliation:
1. E. C. Slater Institute, University of Amsterdam, Plantage Muidergracht 12, 1018 TV Amsterdam, The Netherlands
Publisher
American Chemical Society
Link
https://pubs.acs.org/doi/pdf/10.1021/bk-1998-0711.ch016
Cited by 6 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Role of Local Structure on Catalytic Reactivity: Comparison of Methanol Oxidation by Aqueous Bioinorganic Enzyme Mimic (Vanadium Haloperoxidase) and Vanadia-Based Heterogeneous Catalyst (Supported VO4/SiO2);ACS Catalysis;2019-12-30
2. Vanadium Haloperoxidases;Encyclopedia of Inorganic and Bioinorganic Chemistry;2011-12-15
3. QM/MM investigation of structure and spectroscopic properties of a vanadium-containing peroxidase;Journal of Inorganic Biochemistry;2008-08
4. Vanadium Haloperoxidases;Handbook of Metalloproteins;2006-04-15
5. Cofactor and Substrate Binding to Vanadium Chloroperoxidase Determined by UV−VIS Spectroscopy and Evidence for High Affinity for Pervanadate;Biochemistry;2000-01-13
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