Please use this identifier to cite or link to this item: http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/3956
Title: Kinetics of Melanin Polymerization during Enzymatic and Nonenzymatic Oxidation
Authors: Mondal, Sayan
THAMPI, ARYA
PURANIK, MRINALINI
Dept. of Chemistry
Keywords: Melanin
Biopigment in the animal kingdom
Mechanistic origin
Wavelengths of excitation
Enzyme tyrosinase
2018
Issue Date: Jan-2018
Publisher: American Chemical Society
Citation: Journal of Physical Chemistry B, 122(7), 2047-2063.
Abstract: Melanin is an abundant biopigment in the animal kingdom, but its structure remains poorly understood. This is a substantial impediment to understanding the mechanistic origin of its observed functions. Proposed models of melanin structure include aggregates of both linear and macrocyclic units and noncovalently held monomers. Both models are broadly in agreement with current experimental data. To constrain the structural and kinetic models of melanin, experimental data of high resolution with chemical specificity accompanied by atomistic modeling are required. We have addressed this by obtaining electronic absorption, infrared, and ultraviolet resonance Raman (RR) spectra of melanin at several wavelengths of excitation that are sensitive to small changes in structure. From these experiments, we observed kinetics of the formation of different species en route to melanin polymerization. Exclusive chemical signatures of monomer 3,4-dihydroxyphenylalanine (dopa), intermediate dopachrome (DC), and early-time polymer are established through their vibrational bands at 1292, 1670, and 1616 cm-1 respectively. Direct evidence of reduced heterogeneity of melanin oligomers in tyrosinase-induced formation is provided from experimental measurements of vibrational bandwidths. Models made with density functional theory show that the linear homopolymeric structures of 5,6-dihydroxyindole can account for experimentally observed wavenumbers and broad bandwidth in Raman spectra of dopa-melanin. We capture resonance Raman (RR) signature of DC, the intermediate stabilized by the enzyme tyrosinase, for the first time in an enzyme-assisted melanization reaction using 488 nm excitation wavelength and propose that this wavelength can be used to probe reaction intermediates of melanin formation in solution.
URI: http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/3956
https://doi.org/10.1021/acs.jpcb.7b07941
ISSN: 1520-6106
1520-5207
Appears in Collections:JOURNAL ARTICLES

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