Elsevier

Methods in Enzymology

Volume 400, 2005, Pages 342-359
Methods in Enzymology

Sulfation and Glucuronidation of Phenols: Implications in Coenyzme Q Metabolism

https://doi.org/10.1016/S0076-6879(05)00020-0Get rights and content

Abstract

Phase II conjugation of phenolic compounds constitutes an important mechanism through which exogenous or endogenous toxins are detoxified and excreted. Species differences in the rates of glucuronidation or sulfation can lead to significant variation in the metabolism of this class of compounds. Conjugation of the hydroxyl groups of phenols can occur with glucuronate or sulfate. Quinone metabolism, deactivation, and detoxification are also affected by the same conjugatory systems as phenols; however, reduction of quinones to hydroquinols seems to be a prerequisite. This work reviews current knowledge on phenol conjugation and its implications on hydroquinone metabolism with special consideration for coenzyme Q metabolism.

Section snippets

Phase II Biotransformation of Phenolic Compounds

The ubiquitous appearance of phenols in nature and in industry means that animal exposure from exogenous sources is inevitable. The diverse role of these agents, however, is by no means limited to toxicological importance, as vital and beneficial phenolic compounds (e.g., tyrosine and vitamin E) are also produced endogenously by all living things. Levels of many biogenic and industry‐derived phenolic agents in the body are tightly controlled by bioavailability, amount of exposure, and rate of

Glucuronidation of Phenols

The glucuronidation of phenolic compounds is carried out by glycosyltransferases specifically referred to as UDP‐glucuronosyl transferases (UDPGTs), which are located predominantly in the endoplasmic reticulum. In glucuronidation, glucuronic acid is conjugated to a suitable nucleophilic functional group such as a hydroxyl, amine, or carboxylic acid. UDP‐glucuronic acid is used as the cofactor (Fig. 1).

There are currently two different families of UGTs, which are denoted 1 and 2. In humans,

Sulfation of Phenols

Sulfotransferases (SULTs) are distributed ubiquitously in all animal cells but are particularly concentrated in the liver (Dunn et al., 1998). They catalyze the conjugation of xenobiotics and endobiotics via the formation of sulfate esters on hydrophobic molecules (Fig. 2) or onto protein amino acids in the golgi apparatus. For the purposes of drug and endobiotic sulfation, SULTs localized in the soluble fraction of the cell are categorized as phenol and steroid SULTs. These types are

Quinones in Biology

The ubiquitous appearance of quinones in all organisms is a testament to their fundamental importance in biology. Quinones catalyze important electron transfer reactions, such as those that occur during oxidative phosphorylation and photosynthesis (catalyzed by ubiquinones and plastoquinones, respectively), pyrroloquinoline quinone (PQQ), which is an essential cofactor for bacterial methanol dehydrogenase and glucose dehydrogenase (Duine 1980, Salisbury 1979). Quinones are also formed from the

Sulfate and Glucuronic acid Conjugatory Activity Toward Coenyzme Q (CoQ) Hydroquinone Metabolites

In animals, coenzyme Q plays an important role in the transfer of electrons for various functions, most notably involving the mitochondrial electron transport chain and also for antioxidant protection of membrane components in the cell. Levels of CoQ in the body are most likely maintained by the rate of its synthesis and degradation considering that exogenous CoQ10 in rats has limited bioavailability preferentially partitioning in the spleen and in the liver (Zhang et al., 1996). This is not

References (78)

  • LandiL. et al.

    DT‐Diaphorase maintains the reduced state of ubiquinones in lipid vesicles thereby promoting their antioxidant function

    Free Radic. Biol. Med.

    (1997)
  • LenazG.

    Quinone specificity of complex I

    Biochim. Biophys. Acta

    (1998)
  • MaitiS. et al.

    Stress regulation of sulfotransferases in male rat liver

    Biochem. Biophys. Res. Commun.

    (2004)
  • MarshallA.D. et al.

    Redox control of aryl sulfotransferase specificity

    Arch. Biochem. Biophys.

    (2000)
  • MoridaniM.Y. et al.

    Metabolism of caffeic acid by isolated rat hepatocytes and subcellular fractions

    Toxicol. Lett.

    (2002)
  • OlthofM.R. et al.

    Chlorogenic acid and caffeic acid are absorbed in humans

    J. Nutr.

    (2001)
  • ParrishD.D. et al.

    Activation of CGS 12094 (prinomide metabolite) to 1,4‐benzoquinone by myeloperoxidase: Implications for human idiosyncratic agranulocytosis

    Fundam. Appl. Toxicol.

    (1997)
  • RileyE. et al.

    Isolation and characterisation of a novel rabbit sulfotransferase isoform belonging to the SULT1A subfamily

    Int. J. Biochem. Cell Biol.

    (2002)
  • SaarikoskiS.T. et al.

    Induction of UDP‐glycosyltransferase family 1 genes in rat liver: Different patterns of mRNA expression with two inducers, 3‐methylcholanthrene and beta‐naphthoflavone

    Biochem. Pharmacol.

    (1998)
  • SoarsM.G. et al.

    Cloning and characterization of a canine UDP‐glucuronosyltransferase

    Arch. Biochem. Biophys.

    (2001)
  • ThelinA. et al.

    Half‐life of ubiquinone‐9 in rat tissues

    FEBS Lett.

    (1992)
  • TsoiC. et al.

    Molecular cloning, expression, and characterization of a canine sulfotransferase that is a human ST1B2 ortholog

    Arch. Biochem. Biophys.

    (2001)
  • TsoiC. et al.

    Canine sulfotransferase SULT1A1: Molecular cloning, expression, and characterization

    Arch. Biochem. Biophys.

    (2002)
  • VenkatachalamK.V. et al.

    Isolation, partial purification, and characterization of a novel petromyzonol sulfotransferase from Petromyzon marinus (lamprey) larval liver

    J. Lipid Res.

    (2004)
  • WalleT. et al.

    Evidence of covalent binding of the dietary flavonoid quercetin to DNA and protein in human intestinal and hepatic cells

    Biochem. Pharmacol.

    (2003)
  • YamazoeY. et al.

    Structural similarity and diversity of sulfotransferases

    Chem. Biol. Interact.

    (1994)
  • ZhangY. et al.

    Restricted uptake of dietary coenzyme Q is in contrast to the unrestricted uptake of alpha‐tocopherol into rat organs and cells

    J. Nutr.

    (1996)
  • BlanchardR.L. et al.

    A proposed nomenclature system for the cytosolic sulfotransferase (SULT) superfamily

    Pharmacogenetics

    (2004)
  • BolhaarS.T. et al.

    IgE‐mediated allergy to henna

    Allergy

    (2001)
  • BrixL.A. et al.

    Analysis of the substrate specificity of human sulfotransferases SULT1A1 and SULT1A3: Site‐directed mutagenesis and kinetic studies

    Biochemistry

    (1999)
  • ChanT.S. et al.

    Hepatocyte metabolism of coenzyme Q1 (ubiquinone‐5) to its sulfate conjugate decreases its antioxidant activity

    Biofactors

    (2003)
  • ChanT.S. et al.

    Coenzyme Q cytoprotective mechanisms for mitochondrial complex I cytopathies involves NAD(P)H:quinone oxidoreductase 1(NQO1)

    Free Radic. Res.

    (2002)
  • ChenC. et al.

    Nuclear receptor, pregnane X receptor, is required for induction of UDP‐glucuronosyltranferases in mouse liver by pregnenolone‐16 alpha‐carbonitrile

    Drug Metab. Dispos.

    (2003)
  • ClarkeD.J. et al.

    Cloning of the human UGT1 gene complex in yeast artificial chromosomes: Novel aspects of gene structure and subchromosomal mapping to 2q37

    Biochem. Soc. Trans.

    (1997)
  • CornellB.A. et al.

    Location and activity of ubiquinone 10 and ubiquinone analogues in model and biological membranes

    Biochemistry

    (1987)
  • CourtM.H.

    Acetaminophen UDP‐glucuronosyltransferase in ferrets: Species and gender differences, and sequence analysis of ferret UGT1A6

    J. Vet. Pharmacol. Ther.

    (2001)
  • CourtM.H. et al.

    Molecular genetic basis for deficient acetaminophen glucuronidation by cats: UGT1A6 is a pseudogene, and evidence for reduced diversity of expressed hepatic UGT1A isoforms

    Pharmacogenetics

    (2000)
  • DegliE.M. et al.

    The specificity of mitochondrial complex I for ubiquinones

    Biochem. J.

    (1996)
  • de MoraisS.M. et al.

    Enhanced acetaminophen toxicity in rats with bilirubin glucuronyl transferase deficiency1

    Hepatology

    (1989)

    • Cited by (0)

    View full text
    Copyright © 2005 Elsevier Inc. All rights reserved.