Purification and Properties of Sulfite Oxidase from Different Sources: a Mini Review
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Human Sulfite Oxidase R160Q: Identification of the Mutation in a Sulfite Oxidase-Deficient Patient and Expression and Characterization of the Mutant Enzyme
Proc. Natl. Acad. Sci. USA Vol. 95, pp. 6394–6398, May 1998 Medical Sciences Human sulfite oxidase R160Q: Identification of the mutation in a sulfite oxidase-deficient patient and expression and characterization of the mutant enzyme ROBERT M. GARRETT*†,JEAN L. JOHNSON*, TYLER N. GRAF*, ANNETTE FEIGENBAUM‡, AND K. V. RAJAGOPALAN*§ *Department of Biochemistry, Duke University Medical Center, Durham, NC 27710; and ‡Department of Genetics, The Hospital for Sick Children and University of Toronto, 555 University Avenue, Toronto, ON, Canada M5G 1X8 Edited by Irwin Fridovich, Duke University Medical Center, Durham, NC, and approved March 19, 1998 (received for review February 17, 1998) ABSTRACT Sulfite oxidase catalyzes the terminal reac- tion in the degradation of sulfur amino acids. Genetic defi- ciency of sulfite oxidase results in neurological abnormalities and often leads to death at an early age. The mutation in the sulfite oxidase gene responsible for sulfite oxidase deficiency in a 5-year-old girl was identified by sequence analysis of cDNA obtained from fibroblast mRNA to be a guanine to adenine transition at nucleotide 479 resulting in the amino acid substitution of Arg-160 to Gln. Recombinant protein containing the R160Q mutation was expressed in Escherichia coli, purified, and characterized. The mutant protein con- tained its full complement of molybdenum and heme, but exhibited 2% of native activity under standard assay condi- tions. Absorption spectroscopy of the isolated molybdenum domains of native sulfite oxidase and of the R160Q mutant showed significant differences in the 480- and 350-nm absorp- tion bands, suggestive of altered geometry at the molybdenum center. -
Sulfite Dehydrogenases in Organotrophic Bacteria : Enzymes
Sulfite dehydrogenases in organotrophic bacteria: enzymes, genes and regulation. Dissertation zur Erlangung des akademischen Grades des Doktors der Naturwissenschaften (Dr. rer. nat.) an der Universität Konstanz Fachbereich Biologie vorgelegt von Sabine Lehmann Tag der mündlichen Prüfung: 10. April 2013 1. Referent: Prof. Dr. Bernhard Schink 2. Referent: Prof. Dr. Andrew W. B. Johnston So eine Arbeit wird eigentlich nie fertig, man muss sie für fertig erklären, wenn man nach Zeit und Umständen das möglichste getan hat. (Johann Wolfgang von Goethe, Italienische Reise, 1787) DANKSAGUNG An dieser Stelle möchte ich mich herzlich bei folgenden Personen bedanken: . Prof. Dr. Alasdair M. Cook (Universität Konstanz, Deutschland), der mir dieses Thema und seine Laboratorien zur Verfügung stellte, . Prof. Dr. Bernhard Schink (Universität Konstanz, Deutschland), für seine spontane und engagierte Übernahme der Betreuung, . Prof. Dr. Andrew W. B. Johnston (University of East Anglia, UK), für seine herzliche und bereitwillige Aufnahme in seiner Arbeitsgruppe, seiner engagierten Unter- stützung, sowie für die Übernahme des Koreferates, . Prof. Dr. Frithjof C. Küpper (University of Aberdeen, UK), für seine große Hilfsbereitschaft bei der vorliegenden Arbeit und geplanter Manuskripte, als auch für die mentale Unterstützung während der letzten Jahre! Desweiteren möchte ich herzlichst Dr. David Schleheck für die Übernahme des Koreferates der mündlichen Prüfung sowie Prof. Dr. Alexander Bürkle, für die Übernahme des Prüfungsvorsitzes sowie für seine vielen hilfreichen Ratschläge danken! Ein herzliches Dankeschön geht an alle beteiligten Arbeitsgruppen der Universität Konstanz, der UEA und des SAMS, ganz besonders möchte ich dabei folgenden Personen danken: . Dr. David Schleheck und Karin Denger, für die kritische Durchsicht dieser Arbeit, der durch und durch sehr engagierten Hilfsbereitschaft bei Problemen, den zahlreichen wissenschaftlichen Diskussionen und für die aufbauenden Worte, . -
Inactivation Mechanisms of Alternative Food Processes on Escherichia Coli O157:H7
INACTIVATION MECHANISMS OF ALTERNATIVE FOOD PROCESSES ON ESCHERICHIA COLI O157:H7 DISSERTATION Presented in Partial Fulfillment of the Requirements for the Degree Doctor of Philosophy in the Graduate School of The Ohio State University By Aaron S. Malone, M.S. ***** The Ohio State University 2009 Dissertation Committee: Approved by Professor Ahmed E. Yousef, Adviser Professor Polly D. Courtney ___________________________________ Professor Tina M. Henkin Adviser Food Science and Nutrition Professor Robert Munson ABSTRACT Application of high pressure (HP) in food processing results in a high quality and safe product with minimal impact on its nutritional and organoleptic attributes. This novel technology is currently being utilized within the food industry and much research is being conducted to optimize the technology while confirming its efficacy. Escherichia coli O157:H7 is a well studied foodborne pathogen capable of causing diarrhea, hemorrhagic colitis, and hemolytic uremic syndrome. The importance of eliminating E. coli O157:H7 from food systems, especially considering its high degree of virulence and resistance to environmental stresses, substantiates the need to understand the physiological resistance of this foodborne pathogen to emerging food preservation methods. The purpose of this study is to elucidate the physiological mechanisms of processing resistance of E. coli O157:H7. Therefore, resistance of E. coli to HP and other alternative food processing technologies, such as pulsed electric field, gamma radiation, ultraviolet radiation, antibiotics, and combination treatments involving food- grade additives, were studied. Inactivation mechanisms were investigated using molecular biology techniques including DNA microarrays and knockout mutants, and quantitative viability assessment methods. The results of this research highlighted the importance of one of the most speculated concepts in microbial inactivation mechanisms, the disruption of intracellular ii redox homeostasis. -
Cytochrome C Nitrite Reductase (Ccnir) Does Not Disproportionate Hydroxylamine to Ammonia and Nitrite, Despite a Strongly Favorable Driving Force
Marquette University e-Publications@Marquette Physics Faculty Research and Publications Physics, Department of 4-2014 Shewanella oneidensis Cytochrome c Nitrite Reductase (ccNiR) Does Not Disproportionate Hydroxylamine to Ammonia and Nitrite, Despite a Strongly Favorable Driving Force Matthew Youngblut University of Wisconsin - Milwaukee Daniel J. Pauly University of Wisconsin - Milwaukee Natalia Stein University of Wisconsin - Milwaukee Daniel Walters University of Wisconsin - Milwaukee John A. Conrad University of Wisconsin - Milwaukee See next page for additional authors Follow this and additional works at: https://epublications.marquette.edu/physics_fac Part of the Physics Commons Recommended Citation Youngblut, Matthew; Pauly, Daniel J.; Stein, Natalia; Walters, Daniel; Conrad, John A.; Moran, Graham R.; Bennett, Brian; and Pacheco, A. Andrew, "Shewanella oneidensis Cytochrome c Nitrite Reductase (ccNiR) Does Not Disproportionate Hydroxylamine to Ammonia and Nitrite, Despite a Strongly Favorable Driving Force" (2014). Physics Faculty Research and Publications. 7. https://epublications.marquette.edu/physics_fac/7 Authors Matthew Youngblut, Daniel J. Pauly, Natalia Stein, Daniel Walters, John A. Conrad, Graham R. Moran, Brian Bennett, and A. Andrew Pacheco This article is available at e-Publications@Marquette: https://epublications.marquette.edu/physics_fac/7 Marquette University e-Publications@Marquette Physics Faculty Research and Publications/College of Arts and Sciences This paper is NOT THE PUBLISHED VERSION; but the author’s final, peer-reviewed manuscript. The published version may be accessed by following the link in the citation below. Biochemistry, Vol. 53, No. 13 (8 April 2014): 2136–2144. DOI. This article is © American Chemical Society Publications and permission has been granted for this version to appear in e- Publications@Marquette. American Chemical Society Publications does not grant permission for this article to be further copied/distributed or hosted elsewhere without the express permission from American Chemical Society Publications. -
Amino Acid Disorders
471 Review Article on Inborn Errors of Metabolism Page 1 of 10 Amino acid disorders Ermal Aliu1, Shibani Kanungo2, Georgianne L. Arnold1 1Children’s Hospital of Pittsburgh, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA; 2Western Michigan University Homer Stryker MD School of Medicine, Kalamazoo, MI, USA Contributions: (I) Conception and design: S Kanungo, GL Arnold; (II) Administrative support: S Kanungo; (III) Provision of study materials or patients: None; (IV) Collection and assembly of data: E Aliu, GL Arnold; (V) Data analysis and interpretation: None; (VI) Manuscript writing: All authors; (VII) Final approval of manuscript: All authors. Correspondence to: Georgianne L. Arnold, MD. UPMC Children’s Hospital of Pittsburgh, 4401 Penn Avenue, Suite 1200, Pittsburgh, PA 15224, USA. Email: [email protected]. Abstract: Amino acids serve as key building blocks and as an energy source for cell repair, survival, regeneration and growth. Each amino acid has an amino group, a carboxylic acid, and a unique carbon structure. Human utilize 21 different amino acids; most of these can be synthesized endogenously, but 9 are “essential” in that they must be ingested in the diet. In addition to their role as building blocks of protein, amino acids are key energy source (ketogenic, glucogenic or both), are building blocks of Kreb’s (aka TCA) cycle intermediates and other metabolites, and recycled as needed. A metabolic defect in the metabolism of tyrosine (homogentisic acid oxidase deficiency) historically defined Archibald Garrod as key architect in linking biochemistry, genetics and medicine and creation of the term ‘Inborn Error of Metabolism’ (IEM). The key concept of a single gene defect leading to a single enzyme dysfunction, leading to “intoxication” with a precursor in the metabolic pathway was vital to linking genetics and metabolic disorders and developing screening and treatment approaches as described in other chapters in this issue. -
Molybdenum Cofactor and Sulfite Oxidase Deficiency Jochen Reiss* Institute of Human Genetics, University Medicine Göttingen, Germany
ics: O om pe ol n b A a c t c e e M s s Reiss, Metabolomics (Los Angel) 2016, 6:3 Metabolomics: Open Access DOI: 10.4172/2153-0769.1000184 ISSN: 2153-0769 Research Article Open Access Molybdenum Cofactor and Sulfite Oxidase Deficiency Jochen Reiss* Institute of Human Genetics, University Medicine Göttingen, Germany Abstract A universal molybdenum-containing cofactor is necessary for the activity of all eukaryotic molybdoenzymes. In humans four such enzymes are known: Sulfite oxidase, xanthine oxidoreductase, aldehyde oxidase and a mitochondrial amidoxime reducing component. Of these, sulfite oxidase is the most important and clinically relevant one. Mutations in the genes MOCS1, MOCS2 or GPHN - all encoding cofactor biosynthesis proteins - lead to molybdenum cofactor deficiency type A, B or C, respectively. All three types plus mutations in the SUOX gene responsible for isolated sulfite oxidase deficiency lead to progressive neurological disease which untreated in most cases leads to death in early childhood. Currently, only for type A of the cofactor deficiency an experimental treatment is available. Introduction combination with SUOX deficiency. Elevated xanthine and lowered uric acid concentrations in the urine are used to differentiate this Isolated sulfite oxidase deficiency (MIM#606887) is an autosomal combined form from the isolated SUOX deficiency. Rarely and only in recessive inherited disease caused by mutations in the sulfite oxidase cases of isolated XOR deficiency xanthine stones have been described (SUOX) gene [1]. Sulfite oxidase is localized in the mitochondrial as a cause of renal failure. Otherwise, isolated XOR deficiency often intermembrane space, where it catalyzes the oxidation of sulfite to goes unnoticed. -
Supplementary Material Title Comparative Proteomic Analysis Of
Supplementary Material Title Comparative proteomic analysis of wild-type Physcomitrella patens and an OPDA-deficient Physcomitrella patens mutant with disrupted PpAOS1 and PpAOS2 genes after wounding Authors Weifeng Luoa, Setsuko Komatsub, Tatsuya Abea, Hideyuki Matsuuraa, and Kosaku Takahashia,c* Affiliations aResearch Faculty of Agriculture, Hokkaido University, Sapporo 606-8589, Japan bDepartment of Environmental and Food Sciences, Faculty of Environmental and Information Sciences, Fukui University of Technology, 3-6-1 Gakuen, Fukui 910-8505, Japan cDepartment of Nutritional Science, Faculty of Applied BioScience, Tokyo University of Agriculture, Tokyo 165-8502, Japan. *To whom correspondence should be addressed: Tel.: +81-3-5477-2679; E-mail: [email protected]. Supplementary Fig. S1. Fig. S1. Disruption of PpAOS1 and PpAOS2 genes in P. p a te ns . A, Genomic structures of PpAOS1 and PpAOS2 in the wild-type and targeted PpAOS1 and PpAOS2 knock-out mutants (A5, A19, and A22). The npt II and aph IV expression cassettes were inserted in A5, A19, and A22 strains. B, Genomic PCR data of wild-type, and A5, A19 and A22 strains. P. patens genomic DNA was isolated from protonemata by the CTAB method (Nishiyama et al., Ref. 32). PCR was performed in 50 µL of a reaction mixture containing 1 µL of genomic DNA solution, 1.5 µL of each primer (5 µM), 25 µL of KOD One PCR Master Mix (Toyobo, Japan), and 21 µL of Milli-Q water. PCR was conducted with the following conditions: 30 cycles of 98°C for 10 s, 58°C for 5 s, and 68°C for 15 s. -
The Microbiota-Produced N-Formyl Peptide Fmlf Promotes Obesity-Induced Glucose
Page 1 of 230 Diabetes Title: The microbiota-produced N-formyl peptide fMLF promotes obesity-induced glucose intolerance Joshua Wollam1, Matthew Riopel1, Yong-Jiang Xu1,2, Andrew M. F. Johnson1, Jachelle M. Ofrecio1, Wei Ying1, Dalila El Ouarrat1, Luisa S. Chan3, Andrew W. Han3, Nadir A. Mahmood3, Caitlin N. Ryan3, Yun Sok Lee1, Jeramie D. Watrous1,2, Mahendra D. Chordia4, Dongfeng Pan4, Mohit Jain1,2, Jerrold M. Olefsky1 * Affiliations: 1 Division of Endocrinology & Metabolism, Department of Medicine, University of California, San Diego, La Jolla, California, USA. 2 Department of Pharmacology, University of California, San Diego, La Jolla, California, USA. 3 Second Genome, Inc., South San Francisco, California, USA. 4 Department of Radiology and Medical Imaging, University of Virginia, Charlottesville, VA, USA. * Correspondence to: 858-534-2230, [email protected] Word Count: 4749 Figures: 6 Supplemental Figures: 11 Supplemental Tables: 5 1 Diabetes Publish Ahead of Print, published online April 22, 2019 Diabetes Page 2 of 230 ABSTRACT The composition of the gastrointestinal (GI) microbiota and associated metabolites changes dramatically with diet and the development of obesity. Although many correlations have been described, specific mechanistic links between these changes and glucose homeostasis remain to be defined. Here we show that blood and intestinal levels of the microbiota-produced N-formyl peptide, formyl-methionyl-leucyl-phenylalanine (fMLF), are elevated in high fat diet (HFD)- induced obese mice. Genetic or pharmacological inhibition of the N-formyl peptide receptor Fpr1 leads to increased insulin levels and improved glucose tolerance, dependent upon glucagon- like peptide-1 (GLP-1). Obese Fpr1-knockout (Fpr1-KO) mice also display an altered microbiome, exemplifying the dynamic relationship between host metabolism and microbiota. -
The DMSO Reductase Family of Microbial Molybdenum Enzymes Alastair G
SHOWCASE ON RESEARCH The DMSO Reductase Family of Microbial Molybdenum Enzymes Alastair G. McEwan and Ulrike Kappler Centre for Metals in Biology, School of Molecular and Microbial Sciences, University of Queensland, QLD 4072 Molybdenum is the only element in the second row of led to a division of the oxotransferases into the sulfite transition metals which has a defined role in biology. It dehydrogenase and the dimethylsulfoxide (DMSO) exhibits redox states of (VI), (V) and (IV) within a reductase families (Fig. 1) (4). The Mo hydroxylases biologically-relevant range of redox potentials and is and oxotransferases can act either as dehydrogenases capable of catalysing both oxygen atom transfer and or reductases in catalysis. This reaction can be proton/electron transfer. Apart from nitrogenase, all summarised by the general scheme: + - enzymes containing molybdenum have an active site X + H2O D X=O + 2H + 2e composed of a molybdenum ion coordinated by one or During this process the Mo ion cycles between the two ene-dithiolate (dithiolene) groups that arise from (IV) and (VI) oxidation states with electrons being an unusual organic moiety known as the pterin transferred to or from an electron transfer partner or molybdenum cofactor or pyranopterin (1,2). The substrate. Experiments with xanthine dehydrogenase mononuclear molybdenum enzymes exhibit remarkable using 18O-labelled water have confirmed that the diversity of function and this is in part due to variations oxygen is incorporated into the product during at the Mo active site that are additional to the common substrate oxidation and this distinguishes the core structure. Prior to the appearance of X-ray crystal mononuclear molybdoenzymes from monoxygenases structures of molybdenum enzymes, EPR spectroscopy, where molecular oxygen rather than water acts as an X-ray absorption fine structure spectroscopy (EXAFS) oxygen atom donor (5). -
The Noncanonical Pathway for in Vivo Nitric Oxide Generation: the Nitrate-Nitrite-Nitric Oxide Pathway
1521-0081/72/3/692–766$35.00 https://doi.org/10.1124/pr.120.019240 PHARMACOLOGICAL REVIEWS Pharmacol Rev 72:692–766, July 2020 Copyright © 2020 by The Author(s) This is an open access article distributed under the CC BY-NC Attribution 4.0 International license. ASSOCIATE EDITOR: CHRISTOPHER J. GARLAND The Noncanonical Pathway for In Vivo Nitric Oxide Generation: The Nitrate-Nitrite-Nitric Oxide Pathway V. Kapil, R. S. Khambata, D. A. Jones, K. Rathod, C. Primus, G. Massimo, J. M. Fukuto, and A. Ahluwalia William Harvey Research Institute, Barts and The London School of Medicine and Dentistry, Queen Mary University London, London, United Kingdom (V.K., R.S.K., D.A.J., K.R., C.P., G.M., A.A.) and Department of Chemistry, Sonoma State University, Rohnert Park, California (J.M.F.) Abstract ...................................................................................694 Significance Statement. ..................................................................694 I. Introduction . ..............................................................................694 A. Chemistry of ·NO and Its Metabolism to Nitrite and Nitrate . .........................695 II. Inorganic Nitrite and Nitrate . ............................................................697 A. Historical Uses of Inorganic Nitrite.....................................................697 B. Historical Uses of Inorganic Nitrate ....................................................698 III. Sources and Pharmacokinetics of Nitrate . ................................................698 -
Protein Disulfide Isomerase May Facilitate the Efflux
Redox Biology 1 (2013) 373–380 Contents lists available at SciVerse ScienceDirect Redox Biology journal homepage: www.elsevier.com/locate/redox Protein disulfide isomerase may facilitate the efflux of nitrite derived S-nitrosothiols from red blood cells$ Vasantha Madhuri Kallakunta a, Anny Slama-Schwok b, Bulent Mutus a,n a Department of Chemistry and Biochemistry, University of Windsor, Windsor, Ontario, Canada N9B 3P4 b INRA UR892, Domaine de Vilvert, 78352 Jouy-en-Josas, France article info abstract Article history: Protein disulfide isomerase (PDI) is an abundant protein primarily found in the endoplasmic reticulum Received 20 June 2013 and also secreted into the blood by a variety of vascular cells. The evidence obtained here, suggests that Received in revised form PDI could directly participate in the efflux of NO+ from red blood cells (RBC). PDI was detected both in 8 July 2013 RBC membranes and in the cytosol. PDI was S-nitrosylated when RBCs were exposed to nitrite under Accepted 9 July 2013 ∼50% oxygen saturation but not under ∼100% oxygen saturation. Furthermore, it was observed that hemoglobin (Hb) could promote PDI S-nitrosylation in the presence of ∼600 nM nitrite. In addition, three Keywords: lines of evidence were obtained for PDI–Hb interactions: (1) Hb co-immunoprecipitated with PDI; (2) Hb Nitrite reductase quenched the intrinsic PDI fluorescence in a saturable manner; and (3) Hb–Fe(II)–NO absorption S-nitrosohemoglobin spectrum decreased in a [PDI]-dependent manner. Finally, PDI was detected on the surface RBC under Hypoxic vasodilation ∼100% oxygen saturation and released as soluble under ∼50% oxygen saturation. -
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.