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Photodynamic Effect of Hypericin on the Conformation and Catalytic Activity of Hemoglobin

Hypericin, extracted from H. perforatum, can induce the generation of reactive oxygen species by visible light irradiation, which may consequently induce the conformational change of hemoglobin. We have not only employed UV-vis spectroscopy to observe the changes of UV-vis spectra of the protein, wh...

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Detalles Bibliográficos
Autores principales: Zhao, Jing, Meng, Wenying, Miao, Peng, Yu, Zhiguo, Li, Genxi
Formato: Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2635659/
https://www.ncbi.nlm.nih.gov/pubmed/19325739
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author Zhao, Jing
Meng, Wenying
Miao, Peng
Yu, Zhiguo
Li, Genxi
author_facet Zhao, Jing
Meng, Wenying
Miao, Peng
Yu, Zhiguo
Li, Genxi
author_sort Zhao, Jing
collection PubMed
description Hypericin, extracted from H. perforatum, can induce the generation of reactive oxygen species by visible light irradiation, which may consequently induce the conformational change of hemoglobin. We have not only employed UV-vis spectroscopy to observe the changes of UV-vis spectra of the protein, which reveals the conformational changes of the protein, but also employed electrochemical method to obtain its enhanced peroxidase activity. The photodynamic effect of hypericin on the conformation and catalytic activity of the protein has also been proven to be strongly dependent on the irradiation time, the hypericin concentration and the presence of oxygen. This work is beneficial not only to the fabrication of more sensitive hydrogen peroxide biosensor, but also to the guidance of the usage of this medicinal herb molecule, since the conformational change of the protein and the enhanced peroxidase can be easily obtained only by visible light irradiation on hypericin, the process of which is so common to happen.
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spelling pubmed-26356592009-03-25 Photodynamic Effect of Hypericin on the Conformation and Catalytic Activity of Hemoglobin Zhao, Jing Meng, Wenying Miao, Peng Yu, Zhiguo Li, Genxi Int J Mol Sci Full Research Paper Hypericin, extracted from H. perforatum, can induce the generation of reactive oxygen species by visible light irradiation, which may consequently induce the conformational change of hemoglobin. We have not only employed UV-vis spectroscopy to observe the changes of UV-vis spectra of the protein, which reveals the conformational changes of the protein, but also employed electrochemical method to obtain its enhanced peroxidase activity. The photodynamic effect of hypericin on the conformation and catalytic activity of the protein has also been proven to be strongly dependent on the irradiation time, the hypericin concentration and the presence of oxygen. This work is beneficial not only to the fabrication of more sensitive hydrogen peroxide biosensor, but also to the guidance of the usage of this medicinal herb molecule, since the conformational change of the protein and the enhanced peroxidase can be easily obtained only by visible light irradiation on hypericin, the process of which is so common to happen. Molecular Diversity Preservation International (MDPI) 2008-02-05 /pmc/articles/PMC2635659/ /pubmed/19325739 Text en © 2008 by MDPI
spellingShingle Full Research Paper
Zhao, Jing
Meng, Wenying
Miao, Peng
Yu, Zhiguo
Li, Genxi
Photodynamic Effect of Hypericin on the Conformation and Catalytic Activity of Hemoglobin
title Photodynamic Effect of Hypericin on the Conformation and Catalytic Activity of Hemoglobin
title_full Photodynamic Effect of Hypericin on the Conformation and Catalytic Activity of Hemoglobin
title_fullStr Photodynamic Effect of Hypericin on the Conformation and Catalytic Activity of Hemoglobin
title_full_unstemmed Photodynamic Effect of Hypericin on the Conformation and Catalytic Activity of Hemoglobin
title_short Photodynamic Effect of Hypericin on the Conformation and Catalytic Activity of Hemoglobin
title_sort photodynamic effect of hypericin on the conformation and catalytic activity of hemoglobin
topic Full Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2635659/
https://www.ncbi.nlm.nih.gov/pubmed/19325739
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