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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1985-1-31
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pubmed:abstractText |
A minor pathway for dopamine oxidation to dopaminochrome, by tyrosinase, is proposed. Characterization of intermediates in this oxidative reaction and stoichiometric determination have both been undertaken. After oxidizing dopamine with mushroom tyrosinase or sodium periodate in a pH range from 6.0 to 7.0, it was spectrophotometrically possible to detect o-dopaminoquinone-H+ as the first intermediate in this pathway. The steps for dopamine transformation to dopaminochrome are as follows: dopamine----o-dopaminequinone-H+----o-dopaminequinone---- leukodopaminochrome--- - dopaminochrome. No participation of oxygen was detected in the conversion of leukodopaminochrome to dopaminochrome. Scanning spectroscopy and graphical analysis of the obtained spectra also verified that dopaminequinone-H+ was transformed into aminochrome in a constant ratio. The stoichiometry equation for this conversion is 2 o-dopaminequinone-H+----dopamine + dopaminochrome. The pathway for dopamine oxidation to dopaminochrome by tyrosinase has been studied as a system of various chemical reactions coupled to an enzymatic reaction. A theoretical and experimental kinetic approach is proposed for such a system; this type of mechanism has been named "Enzymatic-chemical-chemical" (EzCC). Rate constants for the implied chemical steps at different pH and temperature values have been evaluated from the measurement of the lag period arising from the accumulation of dopaminochrome that took place when dopamine was oxidized at acid pH. The thermodynamic activation parameters of the chemical steps, the deprotonation of dopaminequinone-H+ to dopaminequinone, and the internal cyclization of dopaminequinone to leukodopaminochrome have been calculated.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Catechol Oxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Monophenol Monooxygenase,
http://linkedlifedata.com/resource/pubmed/chemical/Periodic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Protons,
http://linkedlifedata.com/resource/pubmed/chemical/metaperiodate
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0003-9861
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
235
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
438-48
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:6097187-Basidiomycota,
pubmed-meshheading:6097187-Catechol Oxidase,
pubmed-meshheading:6097187-Chemical Phenomena,
pubmed-meshheading:6097187-Chemistry,
pubmed-meshheading:6097187-Cyclization,
pubmed-meshheading:6097187-Dopamine,
pubmed-meshheading:6097187-Hydrogen-Ion Concentration,
pubmed-meshheading:6097187-Kinetics,
pubmed-meshheading:6097187-Mathematics,
pubmed-meshheading:6097187-Models, Chemical,
pubmed-meshheading:6097187-Monophenol Monooxygenase,
pubmed-meshheading:6097187-Oxidation-Reduction,
pubmed-meshheading:6097187-Periodic Acid,
pubmed-meshheading:6097187-Protons,
pubmed-meshheading:6097187-Spectrophotometry,
pubmed-meshheading:6097187-Temperature
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pubmed:year |
1984
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pubmed:articleTitle |
Chemical intermediates in dopamine oxidation by tyrosinase, and kinetic studies of the process.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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