Iron Complexes Mimicking the Catechol Dioxygenases
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Control of Catechol and Hydroquinone Electron-Transfer Kinetics on Native and Modified Glassy Carbon Electrodes
Anal. Chem. 1999, 71, 4594-4602 Control of Catechol and Hydroquinone Electron-Transfer Kinetics on Native and Modified Glassy Carbon Electrodes Stacy Hunt DuVall and Richard L. McCreery* Department of Chemistry, The Ohio State University, 100 West 18th Avenue, Columbus, Ohio 43210 The electrochemical oxidation of dopamine, 4-methylcat- heterogeneous electron transfer between solid electrodes and echol, dihydroxyphenylacetic acid, dihydroxyphenyl eth- catechols or quinones. Such studies are of fundamental importance ylene glycol, and hydroquinone was examined on several to the electrochemical detection of catecholamines as well as to native and modified glassy carbon (GC) surfaces. Treat- the broader questions about quinone redox chemistry. Notable ment of polished GC with pyridine yielded small ∆Ep examples from the literature are the detailed examination of values for cyclic voltammetry of all systems studied, quinone reduction on platinum in aqueous buffers,7 the oxidation implying fast electron-transfer kinetics. Changes in surface of catechols on carbon paste,2,3 and the dramatic effects of oxide coverage had little effect on kinetics, nor did the adsorbates on quinone electrochemistry on platinum and iridium charge of the catechol species or the solution pH. Small electrodes.5,6,8 These experiments provide an excellent description + - ∆Ep values correlated with catechol adsorption, and of the elementary steps comprising the 2 H ,2e reduction of surface pretreatments that decreased adsorption also an o-orp-quinone to the corresponding hydroquinone and account increased ∆Ep. Electron transfer from catechols was for much of the pH dependence of the observed redox potential profoundly inhibited by a monolayer of nitrophenyl or and kinetics. -
Plant Phenolics: Bioavailability As a Key Determinant of Their Potential Health-Promoting Applications
antioxidants Review Plant Phenolics: Bioavailability as a Key Determinant of Their Potential Health-Promoting Applications Patricia Cosme , Ana B. Rodríguez, Javier Espino * and María Garrido * Neuroimmunophysiology and Chrononutrition Research Group, Department of Physiology, Faculty of Science, University of Extremadura, 06006 Badajoz, Spain; [email protected] (P.C.); [email protected] (A.B.R.) * Correspondence: [email protected] (J.E.); [email protected] (M.G.); Tel.: +34-92-428-9796 (J.E. & M.G.) Received: 22 October 2020; Accepted: 7 December 2020; Published: 12 December 2020 Abstract: Phenolic compounds are secondary metabolites widely spread throughout the plant kingdom that can be categorized as flavonoids and non-flavonoids. Interest in phenolic compounds has dramatically increased during the last decade due to their biological effects and promising therapeutic applications. In this review, we discuss the importance of phenolic compounds’ bioavailability to accomplish their physiological functions, and highlight main factors affecting such parameter throughout metabolism of phenolics, from absorption to excretion. Besides, we give an updated overview of the health benefits of phenolic compounds, which are mainly linked to both their direct (e.g., free-radical scavenging ability) and indirect (e.g., by stimulating activity of antioxidant enzymes) antioxidant properties. Such antioxidant actions reportedly help them to prevent chronic and oxidative stress-related disorders such as cancer, cardiovascular and neurodegenerative diseases, among others. Last, we comment on development of cutting-edge delivery systems intended to improve bioavailability and enhance stability of phenolic compounds in the human body. Keywords: antioxidant activity; bioavailability; flavonoids; health benefits; phenolic compounds 1. Introduction Phenolic compounds are secondary metabolites widely spread throughout the plant kingdom with around 8000 different phenolic structures [1]. -
Study of Ph and Temperature Effect on Lipophilicity of Catechol-Containing Antioxidants by Reversed Phase Liquid Chromatography
Accepted Manuscript Study of pH and temperature effect on lipophilicity of catechol- containing antioxidants by reversed phase liquid chromatography Claver Numviyimana, Tomacz Chmiel, Agata Kot-Wasik, Jacek Namieśnik PII: S0026-265X(18)31156-1 DOI: doi:10.1016/j.microc.2018.10.048 Reference: MICROC 3431 To appear in: Microchemical Journal Received date: 17 September 2018 Revised date: 14 October 2018 Accepted date: 22 October 2018 Please cite this article as: Claver Numviyimana, Tomacz Chmiel, Agata Kot-Wasik, Jacek Namieśnik , Study of pH and temperature effect on lipophilicity of catechol-containing antioxidants by reversed phase liquid chromatography. Microc (2018), doi:10.1016/ j.microc.2018.10.048 This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. ACCEPTED MANUSCRIPT Study of pH and temperature effect on lipophilicity of catechol-containing antioxidants by reversed phase liquid chromatography Claver Numviyimana a,b, Tomacz Chmiel a,*, Agata Kot-Wasik a, Jacek Namieśnik a a Department of Analytical Chemistry, Faculty of Chemistry, Gdansk University of Technology (GUT), 11/12 G. Narutowicza St., 80-233 Gdańsk, Poland b College of Agriculture Animal Sciences and Veterinary Medicine, University of Rwanda (UR-CAVM), Busogo campus, 210 Musanze, Rwanda * Corresponding author: [email protected], Phone: +48-58-347-22-10, Fax: +48-58- 347-26-94. -
Catechol Ortho-Quinones: the Electrophilic Compounds That Form Depurinating DNA Adducts and Could Initiate Cancer and Other Diseases
Carcinogenesis vol.23 no.6 pp.1071–1077, 2002 Catechol ortho-quinones: the electrophilic compounds that form depurinating DNA adducts and could initiate cancer and other diseases Ercole L.Cavalieri1,3, Kai-Ming Li1, Narayanan Balu1, elevated level of reactive oxygen species, a condition known Muhammad Saeed1, Prabu Devanesan1, as oxidative stress (1,2). As electrophiles, catechol quinones Sheila Higginbotham1, John Zhao2, Michael L.Gross2 and can form covalent adducts with cellular macromolecules, Eleanor G.Rogan1 including DNA (4). These are stable adducts that remain in DNA unless removed by repair and depurinating ones that are 1Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, 986805 Nebraska Medical Center, Omaha, released from DNA by destabilization of the glycosyl bond. NE 68198-6805 and 2Department of Chemistry, Washington University, Thus, DNA can be damaged by the reactive quinones them- One Brookings Drive, St Louis, MO 63130, USA selves and by reactive oxygen species (hydroxyl radicals) 3To whom correspondence should be addressed (1,4,5). The formation of depurinating adducts by CE quinones Email: [email protected] reacting with DNA may be a major event in the initiation of Catechol estrogens and catecholamines are metabolized to breast and other human cancers (4,5). The depurinating adducts quinones, and the metabolite catechol (1,2-dihydroxyben- are released from DNA, leaving apurinic sites in the DNA zene) of the leukemogenic benzene can also be oxidized to that can generate -
Mechanistic Study of Cysteine Dioxygenase, a Non-Heme
MECHANISTIC STUDY OF CYSTEINE DIOXYGENASE, A NON-HEME MONONUCLEAR IRON ENZYME by WEI LI Presented to the Faculty of the Graduate School of The University of Texas at Arlington in Partial Fulfillment of the Requirements for the Degree of DOCTOR OF PHILOSOPHY THE UNIVERSITY OF TEXAS AT ARLINGTON August 2014 Copyright © by Student Name Wei Li All Rights Reserved Acknowledgements I would like to thank Dr. Pierce for your mentoring, guidance and patience over the five years. I cannot go all the way through this without your help. Your intelligence and determination has been and will always be an example for me. I would like to thank my committee members Dr. Dias, Dr. Heo and Dr. Jonhson- Winters for the directions and invaluable advice. I also would like to thank all my lab mates, Josh, Bishnu ,Andra, Priyanka, Eleanor, you all helped me so I could finish my projects. I would like to thank the Department of Chemistry and Biochemistry for the help with my academic and career. At Last, I would like to thank my lovely wife and beautiful daughter who made my life meaningful and full of joy. July 11, 2014 iii Abstract MECHANISTIC STUDY OF CYSTEINE DIOXYGENASE A NON-HEME MONONUCLEAR IRON ENZYME Wei Li, PhD The University of Texas at Arlington, 2014 Supervising Professor: Brad Pierce Cysteine dioxygenase (CDO) is an non-heme mononuclear iron enzymes that catalyzes the O2-dependent oxidation of L-cysteine (Cys) to produce cysteine sulfinic acid (CSA). CDO controls cysteine levels in cells and is a potential drug target for some diseases such as Parkinson’s and Alzhermer’s. -
Catalytic Strategies of the Non-Heme Iron Dependent Oxygenases And
Available online at www.sciencedirect.com ScienceDirect Catalytic strategies of the non-heme iron dependent oxygenases and their roles in plant biology Mark D White and Emily Flashman Non-heme iron-dependent oxygenases catalyse the these enzymes play in plant biology. Targeted manipula- incorporation of O2 into a wide range of biological molecules tion of these enzymes could have beneficial effects for and use diverse strategies to activate their substrates. Recent plant growth and/or stress tolerance, addressing the 21st kinetic studies, including in crystallo, have provided century issue of food security. We therefore highlight experimental support for some of the intermediates used by those of potential agricultural (and/or health) interest. different subclasses of this enzyme family. Plant non-heme iron-dependent oxygenases have diverse and important Resolving intermediates in non-heme iron biological roles, including in growth signalling, stress dependent oxygenase catalysis responses and secondary metabolism. Recently identified To activate O2, non-heme iron-dependent oxygenases use roles include in strigolactone biosynthesis, O-demethylation in a redox active iron, coordinated octahedrally at their active morphine biosynthesis and regulating the stability of hypoxia- site with water, usually in a vicinal facial triad arrangement responsive transcription factors. We discuss current structural [1]. During turnover, H2O is sequentially displaced by and mechanistic understanding of plant non-heme iron substrate/co-substrate and O2, which is reductively acti- oxygenases, and how their chemical/genetic manipulation vated enabling a specific substrate modification. Enzyme could have agricultural benefit, for example, for improved yield, subfamilies are proposed to employ different reactive stress tolerance or herbicide development. -
Supporting Information Host-Guest Interactions of Catechol and 4
Electronic Supplementary Material (ESI) for Journal of Materials Chemistry A. This journal is © The Royal Society of Chemistry 2019 Supporting Information Host-Guest Interactions of Catechol and 4-Ethylcatechol with Surface- Immobilized Blue-Box Molecules Ahmed Owais,a,b Alex M. Djerdjev,a James M. Hook,c Alex Yuen,a William Rowlands,d Nicholas G. White,e Chiara Netoa* a School of Chemistry and The University of Sydney Nano Institute, The University of Sydney, NSW 2006 Australia b Renewable Energy Science and Engineering Department, Faculty of Postgraduate Studies for Advanced Sciences (PSAS), Beni-Suef University, Beni-Suef 62511, Egypt c Mark Wainwright Analytical Centre and School of Chemistry, University of New South Wales, Sydney, NSW, 2052, Australia d Licella Pty Ltd, 140 Arthur Street, North Sydney NSW 2060 Australia e Research School of Chemistry, The Australian National University, Canberra, ACT, Australia 1 X-ray crystallography General remarks We grew crystals of 1:1 complexes of BB4+ and catechol from a range of solvents: BB·4Cl·catechol by vapour diffusion of diethyl ether into a methanol solution of the components, BB·4Cl·catechol by vapour diffusion of acetone into a methanol solution of the components and BB·4PF6·catechol by vapour diffusion of diethyl ether into an acetonitrile solution of the components. In some cases, more than one dataset was collected including using synchrotron radiation. Typically, crystals diffracted well, and high-quality diffraction data could be obtained. In all cases, the structure of the macrocycle is clear and typically the anions are also well-defined. In each case, there is an area of electron density within the macrocycle that appears to correspond to a highly disordered catechol molecule (often across a symmetry operation), an example of this is shown in Fig. -
Catalytic Triad' in Directing Promiscuous Substrate-Specificity
Spectroscopic and mechanistic investigation of the enzyme mercaptopropionic acid dioxygenase (MDO), the role of the conserved outer-sphere 'catalytic triad' in directing promiscuous substrate-specificity A DISSERTATION Presented to the faculty of the Graduate School of The University of Texas at Arlington in Partial fulfillment Of the requirements of the Degree of Doctor in Philosophy in CHEMISTRY by SINJINEE SARDAR Under the guidance of Dr. Brad S. Pierce 2nd May, 2018 ACKNOWLEDGEMENT It gives me immense pleasure to thank my compassionate guide Dr. Brad S. Pierce, for his exemplary guidance to accomplish this work. It has been an extraordinary pleasure and privilege to work under his guidance for the past few years. I express my sincere gratitude to my doctoral committee members Prof. Frederick. MacDonnell, Dr. Rasika Dias, and Dr. Jongyun Heo for their valuable advice and constant help. I would also like to thank the Department of Chemistry and Biochemistry of UTA for bestowing me the opportunity to have access to all the departmental facilities required for my work. Here, I express my heartiest gratitude to the ardent and humane guidance of my senior lab mates Dr. Josh Crowell and Dr. Bishnu Subedi which was indispensable. I am immeasurably thankful to my lab mates Wei, Mike, Phil, Nick, Jared and Sydney for their constant support and help. It has been a pleasure to working with all of you. The jokes and laughter we shared have reduced the hardships and stress of graduate school and had made the stressful journey fun. To end with, I utter my heartfelt gratefulness to my parents and my sister for their lifelong support and encouragement which helped me chase my dreams and aspirations and sincere appreciation towards my friends who are my extended family for their lively and spirited encouragement. -
Table II. EPCRA Section 313 Chemical List for Reporting Year 2007 (Including Toxic Chemical Categories)
Table II. EPCRA Section 313 Chemical List For Reporting Year 2007 (including Toxic Chemical Categories) Individually listed EPCRA Section 313 chemicals with CAS numbers are arranged alphabetically starting on page II-3. Following the alphabetical list, the EPCRA Section 313 chemicals are arranged in CAS number order. Covered chemical categories follow. Certain EPCRA Section 313 chemicals listed in Table II have parenthetic “qualifiers.” These qualifiers indicate that these EPCRA Section 313 chemicals are subject to the section 313 reporting requirements if manufactured, processed, or otherwise used in a specific form or when a certain activity is performed. The following chemicals are reportable only if they are manufactured, processed, or otherwise used in the specific form(s) listed below: Chemical CAS Number Qualifier Aluminum (fume or dust) 7429-90-5 Only if it is a fume or dust form. Aluminum oxide (fibrous forms) 1344-28-1 Only if it is a fibrous form. Ammonia (includes anhydrous ammonia and aqueous ammonia 7664-41-7 Only 10% of aqueous forms. 100% of from water dissociable ammonium salts and other sources; 10 anhydrous forms. percent of total aqueous ammonia is reportable under this listing) Asbestos (friable) 1332-21-4 Only if it is a friable form. Hydrochloric acid (acid aerosols including mists, vapors, gas, 7647-01-0 Only if it is an aerosol form as fog, and other airborne forms of any particle size) defined. Phosphorus (yellow or white) 7723-14-0 Only if it is a yellow or white form. Sulfuric acid (acid aerosols including mists, vapors, gas, fog, and 7664-93-9 Only if it is an aerosol form as other airborne forms of any particle size) defined. -
Structural and Mechanistic Studies on 2-Oxoglutarate-Dependent Oxygenases and Related Enzymes Christopher J Schofield and Zhihong Zhang
722 Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes Christopher J Schofield and Zhihong Zhang Mononuclear nonheme-Fe(II)-dependent oxygenases comprise The 2OG-dependent oxygenases have emerged as the an extended family of oxidising enzymes, of which the largest known family of nonheme oxidising enzymes [7,8] 2-oxoglutarate-dependent oxygenases and related enzymes are (Figure 1a). Their occurrence is ubiquitous, having been the largest known subgroup. Recent crystallographic and identified in many organisms ranging from prokaryotes to mechanistic studies have helped to define the overall fold of eukaryotes. Recent evidence also indicates that a 2OG- the 2-oxoglutarate-dependent enzymes and have led to the dependent oxygenase, prolyl 4-hydroxylase, is expressed by identification of coordination chemistry closely related to that of the P. bursaria Chlorella virus-1 [9]. Oxidative reactions catal- other nonheme-Fe(II)-dependent oxygenases, suggesting ysed by 2OG-dependent dioxygenases are steps in the related mechanisms for dioxygen activation that involve iron- biosynthesis of a variety of metabolites, including materials mediated electron transfer. of medicinal or agrochemical importance, such as plant ‘hor- mones’ (e.g. gibberellins) and antibiotics (e.g. cephalosporins Address and the β-lactamase inhibitor clavulanic acid). The Oxford Centre for Molecular Sciences and the Department of Chemistry, The Dyson Perrins Laboratory, South Parks Road, Oxford In mammals, the best-characterised 2OG-dependent oxy- OX1 3QY, UK genase is prolyl-4-hydroxylase, which catalyses the Current Opinion in Structural Biology 1999, 9:722–731 post-translational hydroxylation of proline residues in col- lagen. Mammalian prolyl-4-hydroxylase is an α β 0959-440X/99/$ — see front matter © 1999 Elsevier Science Ltd. -
Assay for Catechol Peroxidase Compounds Using 1,2
ANALYTICAL SCIENCES JUNE 1991, VOL. 7 437 Assay for Peroxidase Using 1,2-Diarylethylenediamines and Catechol Compounds as Fluorogenic Substrates Hitoshi NoHTA, Tomohiro WATANABE,Hiroaki NAGAOKAand YOsuke OHKURAt Faculty of Pharmaceutical Sciences, Kyushu University62, Maidashi, Fukuoka 812, Japan A novel method for the fluorometric assay of horseradish peroxidase and microperoxidase activities is described based on their catalytic reactions between 1,2-diarylethylenediamines and catechol compounds as fluorogenic substrates in the presence of hydrogen peroxide. meso-l,2-Diphenylethylenediamine and epinephrine as a couple of substrates are most recommendable in practical use. This method is highly sensitive: the detection limits (S/ N=2) are 10 µU tube-1 for horseradish peroxidase and 500 fmol tube-1 for microperoxidase. Keywords Horseradish peroxidase, microperoxidase, activity assay, fluorometry, 1,2-diarylethylenediamine, meso- 1,2-diphenylethylenediamine, epinephrine Peroxidase has been used as a marker enzyme in previously: ss DPE, 1,2-bis(2-hydroxyphenyl)ethylene- immunoassay and DNA hybridization assay because of diamine, 1,2-bis(2-, 3- and 4-methoxyphenyl)ethylene- its high stability. Activity is commonly assayed by diamines, 1,2-bis(2- and 4-ethoxyphenyl)ethylenedi- colorimetric or fluorometric methods: the former uses amines, 1,2-bis(2-, 3- and 4-methylphenyl)ethylenedi- 4-aminoantipyrine-phenols, 2,2'-azino-di(3-ethylbenzo- amines, 1,2-bis(4-ethylphenyl)ethylenediamine, 1,2- thiazoline-6-sulfonic acid)2, benzidine3 or di-o-anisi- bis(3,4-dimethoxyphenyl)ethylenediamine, 1,2-bis(3,4- dine;4 the latter uses p-substituted phenolic compounds, methylenedioxyphenyl)ethylenediamine, 1,2-bis(4- such as homovanillic acids, tyramine6, p-cresol' and p- fluorophenyl)ethylenediamine, 1,2-bis(2-, 3- and 4- hydroxyphenylpropionic acids as substrates. -
University of Groningen Exploring the Cofactor-Binding and Biocatalytic
University of Groningen Exploring the cofactor-binding and biocatalytic properties of flavin-containing enzymes Kopacz, Malgorzata IMPORTANT NOTE: You are advised to consult the publisher's version (publisher's PDF) if you wish to cite from it. Please check the document version below. Document Version Publisher's PDF, also known as Version of record Publication date: 2014 Link to publication in University of Groningen/UMCG research database Citation for published version (APA): Kopacz, M. (2014). Exploring the cofactor-binding and biocatalytic properties of flavin-containing enzymes. Copyright Other than for strictly personal use, it is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), unless the work is under an open content license (like Creative Commons). The publication may also be distributed here under the terms of Article 25fa of the Dutch Copyright Act, indicated by the “Taverne” license. More information can be found on the University of Groningen website: https://www.rug.nl/library/open-access/self-archiving-pure/taverne- amendment. Take-down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim. Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal. For technical reasons the number of authors shown on this cover page is limited to 10 maximum. Download date: 29-09-2021 Exploring the cofactor-binding and biocatalytic properties of flavin-containing enzymes Małgorzata M. Kopacz The research described in this thesis was carried out in the research group Molecular Enzymology of the Groningen Biomolecular Sciences and Biotechnology Institute (GBB), according to the requirements of the Graduate School of Science, Faculty of Mathematics and Natural Sciences.