F
Francisco Garcia-Molina
Researcher at University of Murcia
Publications - 63
Citations - 1851
Francisco Garcia-Molina is an academic researcher from University of Murcia. The author has contributed to research in topics: Tyrosinase & Michaelis–Menten kinetics. The author has an hindex of 21, co-authored 60 publications receiving 1427 citations. Previous affiliations of Francisco Garcia-Molina include University of Castilla–La Mancha.
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Journal ArticleDOI
A comprehensive review on tyrosinase inhibitors.
Samaneh Zolghadri,Asieh Bahrami,Mahmud Tareq Hassan Khan,Jose Munoz-Munoz,Francisco Garcia-Molina,Francisco García-Cánovas,Ali Akbar Saboury +6 more
TL;DR: This review has focused on the tyrosinase inhibitors discovered from all sources and biochemically characterised in the last four decades.
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A Review on Spectrophotometric Methods for Measuring the Monophenolase and Diphenolase Activities of Tyrosinase
Francisco Garcia-Molina,J. L. Muñoz,Ramón Varón,José Neptuno Rodríguez-López,Francisco García-Cánovas,José Tudela +5 more
TL;DR: The analytical and numerical solutions to the system of differential equations corresponding to the reaction mechanism of each case confirm the underlying validity of the different spectrophotometric methods proposed for the kinetic characterization of tyrosinase in its action on different substrates.
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Calculating molar absorptivities for quinones: application to the measurement of tyrosinase activity.
J.L. Muñoz,Francisco Garcia-Molina,Ramón Varón,José Neptuno Rodríguez-López,F. García-Cánovas,José Tudela +5 more
TL;DR: Several methods for following tyrosinase activity are proposed, and a kinetic characterization of the enzyme's action on these substrates is made, showing several advantages over the enzymatic method.
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Mushroom tyrosinase: catalase activity, inhibition, and suicide inactivation.
Francisco Garcia-Molina,Alexander N.P. Hiner,Lorena G. Fenoll,José Neptuno Rodríguez-López,Pedro Antonio García-Ruiz,Francisco García-Cánovas,José Tudela +6 more
TL;DR: Catalase activity is favored by increased pH, with an optimum at pH = 6.4, and chloride, which binds in the equatorial orientation to the protonated enzyme (E(m)H), inhibits both catalase and diphenolase activities.
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Michaelis constants of mushroom tyrosinase with respect to oxygen in the presence of monophenols and diphenols.
Lorena G. Fenoll,José Neptuno Rodríguez-López,Francisco Garcia-Molina,Francisco García-Cánovas,José Tudela +4 more
TL;DR: The theoretical values of K(mO(2) from the experimental values of catalytic constants and k(+8) towards several monophenols and o-diphenols are calculated and the reliability and the significance of the values are discussed.