
doi: 10.1248/cpb.37.3386
pmid: 2517246
The oxidation of tyrosine by monophenol monooxygenase (tyrosinase: EC 1.10.3.1) to melanin has been studied by a combination of ultraviolet, circular dichroism, and nuclear magnetic resonance techniques. It is demonstrated that the chiral intermediate (dopachrome) is generated stereoselectively in this enzymic reaction.
Melanins, stereoselective reaction, Magnetic Resonance Spectroscopy, Chemical Phenomena, dopa, Circular Dichroism, Molecular Conformation, chiral intermediate, dopachrome, tyrosinase, melanin, Chemistry, Spectrophotometry, Ultraviolet, tyrosine, Catechol Oxidase
Melanins, stereoselective reaction, Magnetic Resonance Spectroscopy, Chemical Phenomena, dopa, Circular Dichroism, Molecular Conformation, chiral intermediate, dopachrome, tyrosinase, melanin, Chemistry, Spectrophotometry, Ultraviolet, tyrosine, Catechol Oxidase
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