a role of proton transfer in peroxidase-catalyzed process elucidated by substrates docking calculations质子转移的角色peroxidase-catalyzed过程阐明基质对接计算.pdfVIP

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a role of proton transfer in peroxidase-catalyzed process elucidated by substrates docking calculations质子转移的角色peroxidase-catalyzed过程阐明基质对接计算.pdf

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a role of proton transfer in peroxidase-catalyzed process elucidated by substrates docking calculations质子转移的角色peroxidase-catalyzed过程阐明基质对接计算

BMC Structural Biology BioMed Central BMC Structural Biology :3 2001, 1 Research article A role of proton transfer in peroxidase-catalyzed process elucidated by substrates docking calculations 1 2 Juozas Kulys* and Arturas Ziemys Address: 1Department of Enzyme Chemistry, Institute of Biochemistry, Mokslininku 12, Vilnius, 2600, Lithuania and 2Department of Biology, Faculty of Natural Sciences Vytautas Magnus University, Vileikos 8, Kaunas, 3500, Lithuania E-mail: Juozas Kulys* - jkulys@bchi.lt; Arturas Ziemys - a3arzi@vaidila.vdu.lt *Corresponding author Published: 28 August 2001 Received: 5 July 2001 Accepted: 28 August 2001 BMC Structural Biology 2001, 1:3 This article is available from: /1472-6807/1/3 © 2001 Kulys and Ziemys; licensee BioMed Central Ltd. Verbatim copying and redistribution of this article are permitted in any medium for any non- commercial purpose, provided this notice is preserved along with the articles original URL. For commercial use, contact info@ Abstract Background: Previous kinetic investigations of fungal-peroxidase catalyzed oxidation of N-aryl hydroxamic acids (AHAs) and N-aryl-N-hydroxy urethanes (AHUs) revealed that the rate of reaction was independent of the formal redox potential of substrates. Moreover, the oxidation rate was 3–5 orders of magnitude less than for oxidation of physiological phenol substrates, though the redox potential was similar. Results: To explain the unexpectedly low reactivity of AHAs and AHUs we mad