Catalysis and inactivation of tyrosinase in its action on hydroxyhydroquinone

Maria del Mar Garcia-Molina; Jose Luis Muñoz-Muñoz; Jose Berna; Pedro Antonio García-Ruiz; Jose Neptuno Rodriguez-Lopez; Francisco Garcia-Canovas

doi:10.1002/iub.1250

Catalysis and inactivation of tyrosinase in its action on hydroxyhydroquinone

Maria del Mar Garcia-Molina, Jose Luis Muñoz-Muñoz, Jose Berna, Pedro Antonio García-Ruiz, Jose Neptuno Rodriguez-Lopez, Francisco Garcia-Canovas

Applied Sciences

Research output: Contribution to journal › Article › peer-review

6 Citations (Scopus)

Abstract

Hydroxyhydroquinone (HHQ) was characterized kinetically as a tyrosinase substrate. A kinetic mechanism is proposed, in which HHQ is considered as a monophenol or as an o-diphenol, depending on the part of the molecule that interacts with the enzyme. The kinetic parameters obtained from an analysis of the measurements of the initial steady state rate of 2-hydroxy p-benzoquinone formation were kcatapp=229.0±7.7 s(-1) and KMapp,HHQ=0.40±0.05 mM. Furthermore, the action of tyrosinase on HHQ led to the enzyme's inactivation through a suicide inactivation mechanism. This suicide inactivation process was characterized kinetically by λmaxapp (the apparent maximum inactivation constant) and r, the number of turnovers made by 1 mol of enzyme before being inactivated. The values of λmaxapp and r were (8.2±0.1)×10(-3) s(-1) and 35,740±2,548, respectively.

Original language	English
Pages (from-to)	122-127
Journal	IUBMB Life
Volume	66
Issue number	2
Early online date	27 Feb 2014
DOIs	https://doi.org/10.1002/iub.1250
Publication status	Published - Feb 2014

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@article{cd0e7e865f314821a6ddf522e4ba1d17,

title = "Catalysis and inactivation of tyrosinase in its action on hydroxyhydroquinone",

abstract = "Hydroxyhydroquinone (HHQ) was characterized kinetically as a tyrosinase substrate. A kinetic mechanism is proposed, in which HHQ is considered as a monophenol or as an o-diphenol, depending on the part of the molecule that interacts with the enzyme. The kinetic parameters obtained from an analysis of the measurements of the initial steady state rate of 2-hydroxy p-benzoquinone formation were kcatapp=229.0±7.7 s(-1) and KMapp,HHQ=0.40±0.05 mM. Furthermore, the action of tyrosinase on HHQ led to the enzyme's inactivation through a suicide inactivation mechanism. This suicide inactivation process was characterized kinetically by λmaxapp (the apparent maximum inactivation constant) and r, the number of turnovers made by 1 mol of enzyme before being inactivated. The values of λmaxapp and r were (8.2±0.1)×10(-3) s(-1) and 35,740±2,548, respectively.",

keywords = "Agaricales/enzymology, Catalysis, Catechol Oxidase/metabolism, Hydrogen-Ion Concentration, Hydroquinones/metabolism, Kinetics, Monophenol Monooxygenase/chemistry, Oxidation-Reduction, Phenols",

author = "{del Mar Garcia-Molina}, Maria and Mu{\~n}oz-Mu{\~n}oz, {Jose Luis} and Jose Berna and Garc{\'i}a-Ruiz, {Pedro Antonio} and Rodriguez-Lopez, {Jose Neptuno} and Francisco Garcia-Canovas",

note = "{\textcopyright} 2014 International Union of Biochemistry and Molecular Biology.",

year = "2014",

month = feb,

doi = "10.1002/iub.1250",

language = "English",

volume = "66",

pages = "122--127",

journal = "IUBMB Life",

issn = "1521-6543",

publisher = "Wiley",

number = "2",

}

TY - JOUR

T1 - Catalysis and inactivation of tyrosinase in its action on hydroxyhydroquinone

AU - del Mar Garcia-Molina, Maria

AU - Muñoz-Muñoz, Jose Luis

AU - Berna, Jose

AU - García-Ruiz, Pedro Antonio

AU - Rodriguez-Lopez, Jose Neptuno

AU - Garcia-Canovas, Francisco

PY - 2014/2

Y1 - 2014/2

N2 - Hydroxyhydroquinone (HHQ) was characterized kinetically as a tyrosinase substrate. A kinetic mechanism is proposed, in which HHQ is considered as a monophenol or as an o-diphenol, depending on the part of the molecule that interacts with the enzyme. The kinetic parameters obtained from an analysis of the measurements of the initial steady state rate of 2-hydroxy p-benzoquinone formation were kcatapp=229.0±7.7 s(-1) and KMapp,HHQ=0.40±0.05 mM. Furthermore, the action of tyrosinase on HHQ led to the enzyme's inactivation through a suicide inactivation mechanism. This suicide inactivation process was characterized kinetically by λmaxapp (the apparent maximum inactivation constant) and r, the number of turnovers made by 1 mol of enzyme before being inactivated. The values of λmaxapp and r were (8.2±0.1)×10(-3) s(-1) and 35,740±2,548, respectively.

AB - Hydroxyhydroquinone (HHQ) was characterized kinetically as a tyrosinase substrate. A kinetic mechanism is proposed, in which HHQ is considered as a monophenol or as an o-diphenol, depending on the part of the molecule that interacts with the enzyme. The kinetic parameters obtained from an analysis of the measurements of the initial steady state rate of 2-hydroxy p-benzoquinone formation were kcatapp=229.0±7.7 s(-1) and KMapp,HHQ=0.40±0.05 mM. Furthermore, the action of tyrosinase on HHQ led to the enzyme's inactivation through a suicide inactivation mechanism. This suicide inactivation process was characterized kinetically by λmaxapp (the apparent maximum inactivation constant) and r, the number of turnovers made by 1 mol of enzyme before being inactivated. The values of λmaxapp and r were (8.2±0.1)×10(-3) s(-1) and 35,740±2,548, respectively.

KW - Agaricales/enzymology

KW - Catalysis

KW - Catechol Oxidase/metabolism

KW - Hydrogen-Ion Concentration

KW - Hydroquinones/metabolism

KW - Kinetics

KW - Monophenol Monooxygenase/chemistry

KW - Oxidation-Reduction

KW - Phenols

U2 - 10.1002/iub.1250

DO - 10.1002/iub.1250

M3 - Article

C2 - 24578277

VL - 66

SP - 122

EP - 127

JO - IUBMB Life

JF - IUBMB Life

SN - 1521-6543

IS - 2

ER -