Hydrogen Peroxide Helps in the Identification of Monophenols as Possible Substrates of Tyrosinase
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- GARCÍA-MOLINA Mary of the Sea
- GENZ: Investigation Group of Enzimology, Department of Biochemistry and Molecular Biology A. Faculty of Biology, Regional Campus of International Excellence ``Campus Mare Nostrum'', University of Murcia
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- MUÑOZ-MUÑOZ Joseph Luis
- GENZ: Investigation Group of Enzimology, Department of Biochemistry and Molecular Biology A. Faculty of Biology, Regional Campus of International Excellence ``Campus Mare Nostrum'', University of Murcia
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- BERNA Joseph
- Group of Synthetic Organic Chemistry, Department of Organic Chemistry, Faculty of Chemistry, Regional Campus of International Excellence ``Campus Mare Nostrum'', University of Murcia
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- RODRÍGUEZ-LÓPEZ Joseph Neptune
- GENZ: Investigation Group of Enzimology, Department of Biochemistry and Molecular Biology A. Faculty of Biology, Regional Campus of International Excellence ``Campus Mare Nostrum'', University of Murcia
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- VARÓN Ramón
- Department of Physical Chemistry, Upper Polytechnic School, University of Castilla la Mancha, Spain Avenue s/n, University Campus
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- GARCÍA-CÁNOVAS Francis
- GENZ: Investigation Group of Enzimology, Department of Biochemistry and Molecular Biology A. Faculty of Biology, Regional Campus of International Excellence ``Campus Mare Nostrum'', University of Murcia
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Abstract
Tyrosinase exists in three forms in the catalytic cycle depending on the oxidation state of the copper: met- (Em), oxy- (Eox), and deoxy- (Ed). When O-quinones, products of the enzymatic reaction, evolve chemically to generate an O-diphenol in the reaction medium, the enzyme acts on a monophenol with O-diphenol as reductant, converting Em to Ed. The binding of Ed to molecular oxygen gives Eox, which is active on monophenols, but when the O-quinone product does not generate O-diphenol through chemical evolution, the monophenol does not act as an enzyme substrate. The fact that Eox can be formed from Em with hydrogen peroxide can be used to help identify whether a monophenol is a substrate of tyrosinase. The results obtained in this study confirm that compounds previously described as inhibitors of the enzyme are true substrates of it.
Journal
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 77 (12), 2383-2388, 2013
Japan Society for Bioscience, Biotechnology, and Agrochemistry
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Keywords
Details 詳細情報について
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- CRID
- 1390001206479128960
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- NII Article ID
- 130003381952
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- NII Book ID
- AA10824164
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- COI
- 1:STN:280:DC%2BC2c3ks1amtA%3D%3D
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- ISSN
- 13476947
- 09168451
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- NDL BIB ID
- 025124241
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- PubMed
- 24317051
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- Abstract License Flag
- Disallowed