Effect of ferrous ions on the monophenolase activity of tyrosinase

Ros, JoséRamón; Rodríguez-López, JoséNeptuno; Garcı́a-Cánovas, Francisco

doi:10.1016/0167-4838(93)90166-o

Cited by 11 publications

(11 citation statements)

References 27 publications

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“…An LMCT band was observed for the resulting films ( Figure S11), suggesting the formation of ironcatechol complexes during stage II. Theaddition of FeCl 2 can both enhance the catalytic performance of tyrosinase by promoting hydroxylation of tyrosine [25] and provide iron ions to chelate catechol-containing molecules in solution. [26] This is confirmed by the control experiments,w hich demonstrated that the film formed after incubation for 3h solely with tyrosinase in the absence of FeCl 2 has atotal thickness (stage I and stage II) of % 12.1 nm.…”

Section: Resultsmentioning

confidence: 99%

Expanding the Toolbox of Metal–Phenolic Networks via Enzyme‐Mediated Assembly

Zhong

Richardson

et al. 2019

Angew Chem Int Ed

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Functional coatings are of considerable interest because of their fundamental implications for interfacial assembly and promise for numerous applications.Universally adherent materials have recently emerged as versatile functional coatings;however,such coatings are generally limited to catechol, (ortho-diphenol)-containing molecules,a sb uilding blocks.H ere,w er eport af acile,b iofriendly enzyme-mediated strategy for assembling aw ide range of molecules (e.g., 14 representative molecules in this study) that do not natively have catechol moieties,i ncluding small molecules,p eptides,a nd proteins,o nv arious surfaces,w hile preserving the molecules inherent function, such as catalysis ( % 80 %r etention of enzymatic activity for trypsin). Assembly is achieved by in situ conversion of monophenols into catechols via tyrosinase, where films form on surfaces via covalent and coordination cross-linking.T he resulting coatings are robust, functional (e.g., in protective coatings,biological imaging, and enzymatic catalysis), and versatile for diverse secondary surface-confined reactions (e.g., biomineralization, metal ion chelation, and N-hydroxysuccinimide conjugation).

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Section: Resultsmentioning

confidence: 99%

Expanding the Toolbox of Metal–Phenolic Networks via Enzyme‐Mediated Assembly

Zhong

Richardson

et al. 2019

Angew Chem Int Ed

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“…In the kinetic studies, lag time is the time required for the resting met form to be drawn into the active deoxy form by the reducing agent, arising via action of the small amounts of the oxy form that usually accompany the met form. In the presence of reducing agents known as cofactors, especially o-diphenol derivatives such as L-DOPA and (+)-catechin, tyrosinase was activated and the lag time was shortened or abolished as shown in figure 2 [38,46,47]. L-DOPA at a very low concentration was the most effective reducing agent for eliminating lag time.…”

Section: Mechanism Of Tyrosinase Actionmentioning

confidence: 95%

“…Kinetic studies of the steady state of the pathway show the lower catalytic efficiency of tyrosinase on monophenols than on o-diphenols [35,44,45]. Monophenolase activity is typically characterized by a lag time [42,43,46,47] which is dependent on factors such as substrate and enzyme concentrations, and presence of a hydrogen donor [6]. In the kinetic studies, lag time is the time required for the resting met form to be drawn into the active deoxy form by the reducing agent, arising via action of the small amounts of the oxy form that usually accompany the met form.…”

Section: Mechanism Of Tyrosinase Actionmentioning

confidence: 99%

Tyrosinase inhibitors from natural and synthetic sources: structure, inhibition mechanism and perspective for the future

Kim

Uyama

2005

CMLS, Cell. Mol. Life Sci.

918

698

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Tyrosinase is known to be a key enzyme in melanin biosynthesis, involved in determining the color of mammalian skin and hair. Various dermatological disorders, such as melasma, age spots and sites of actinic damage, arise from the accumulation of an excessive level of epidermal pigmentation. In addition, unfavorable enzymatic browning of plant-derived foods by tyrosinase causes a decrease in nutritional quality and economic loss of food products. The inadequacy of current conventional techniques to prevent tyrosinase action encourages us to seek new potent tyrosinase inhibitors. This article overviews the various inhibitors obtained from natural and synthetic sources with their industrial importance.

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“…An LMCT band was observed for the resulting films (Figure S11), suggesting the formation of iron–catechol complexes during stage II. The addition of FeCl 2 can both enhance the catalytic performance of tyrosinase by promoting hydroxylation of tyrosine and provide iron ions to chelate catechol‐containing molecules in solution . This is confirmed by the control experiments, which demonstrated that the film formed after incubation for 3 h solely with tyrosinase in the absence of FeCl 2 has a total thickness (stage I and stage II) of ≈12.1 nm.…”

Section: Resultsmentioning

confidence: 99%

Expanding the Toolbox of Metal–Phenolic Networks via Enzyme‐Mediated Assembly

Zhong

Richardson

et al. 2019

Angewandte Chemie

View full text Add to dashboard Cite

Functional coatings are of considerable interest because of their fundamental implications for interfacial assembly and promise for numerous applications.Universally adherent materials have recently emerged as versatile functional coatings;however,such coatings are generally limited to catechol, (ortho-diphenol)-containing molecules,a sb uilding blocks.H ere,w er eport af acile,b iofriendly enzyme-mediated strategy for assembling aw ide range of molecules (e.g., 14 representative molecules in this study) that do not natively have catechol moieties,i ncluding small molecules,p eptides,a nd proteins,o nv arious surfaces,w hile preserving the molecules inherent function, such as catalysis (% 80 %r etention of enzymatic activity for trypsin). Assembly is achieved by in situ conversion of monophenols into catechols via tyrosinase, where films form on surfaces via covalent and coordination cross-linking.T he resulting coatings are robust, functional (e.g., in protective coatings,biological imaging, and enzymatic catalysis), and versatile for diverse secondary surface-confined reactions (e.g., biomineralization, metal ion chelation, and N-hydroxysuccinimide conjugation).

show abstract

Effect of ferrous ions on the monophenolase activity of tyrosinase

Cited by 11 publications

References 27 publications

Expanding the Toolbox of Metal–Phenolic Networks via Enzyme‐Mediated Assembly

Expanding the Toolbox of Metal–Phenolic Networks via Enzyme‐Mediated Assembly

Tyrosinase inhibitors from natural and synthetic sources: structure, inhibition mechanism and perspective for the future

Expanding the Toolbox of Metal–Phenolic Networks via Enzyme‐Mediated Assembly

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