Oxidation of catechols and catecholamines by horseradish peroxidase and lactoperoxidase: ESR spin stabilization approach combined with optical methods |
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| Institution: | 1. School of Family and Consumer Sciences, 875 Perimeter Drive, MS 3183, University of Idaho, Moscow, ID 83843-3183, USA;2. Division of Soil & Land Resources, 875 Perimeter Drive, MS 2339, University of Idaho, Moscow, ID 83844-2339, USA;3. Agriculture International Programs, 875 Perimeter Drive, MS 2331, University of Idaho, Moscow, ID 83844-2331, USA;1. “Raluca Ripan” Institute for Research in Chemistry, “Babes- Bolyai” University, Fântânele Str. no. 30, 400294 Cluj-Napoca, Romania;2. Electronic Microscopy Centre, “Babes- Bolyai” University, 5-7 Clinicilor, 400006 Cluj-Napoca, Romania;3. National Institute for Research and Development of Isotopic and Molecular Technologies, 65-103 Donath, 400293 Cluj-Napoca, Romania;1. Center for Shockwave Medicine and Tissue Engineering, Department of Medical Research, Kaohsiung Chang Gung Memorial Hospital and Chang Gung University College of Medicine, Kaohsiung, Taiwan;2. Department of Food Science, National Pingtung University of Science and Technology, Pingtung, Taiwan;3. Department of Chinese Pharmaceutical Science and Chinese Medicine Resources, China Medical University, Taichung, Taiwan;1. Jožef Stefan Institute, Jamova 39, Ljubljana 1000, Slovenia;2. Faculty of Mathematics and Physics, University of Ljubljana, Jadranska 19, Ljubljana 1000, Slovenia;3. Agricultural Institute of Slovenia, Hacquetova 17, Ljubljana 1000, Slovenia |
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| Abstract: | Oxidation of catechols and catecholamines by horseradish peroxidase (HRP) and lactoperoxidase (LPO) has been studied by electron spin resonance (ESR) and electronic spectroscopies. The ESR technique has been used as an ESR spin stabilization approach by complexation of o-semiquinone free radicals with ZnII ions. ESR spectra and parameters of these free radical complexed forms are in good agreement with those obtained previously for complexed and uncomplexed species. The Km values obtained with the two methods show stereoselective effects towards the chiral substrates l- and d-dopa from HRP and LPO. Furthermore, these enzymes display opposite stereochemical interactions, in agreement with the analogous effects observed on l- and d-tyrosine by electronic and NMR binding studies. |
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