Flavins and Flavoproteins 1999
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METACYC ID Description A0AR23 GO:0004842 (Ubiquitin-Protein Ligase
Electronic Supplementary Material (ESI) for Integrative Biology This journal is © The Royal Society of Chemistry 2012 Heat Stress Responsive Zostera marina Genes, Southern Population (α=0. -
Biochemical and Biophysical Characterisation of Anopheles Gambiae Nadph-Cytochrome P450 Reductase
BIOCHEMICAL AND BIOPHYSICAL CHARACTERISATION OF ANOPHELES GAMBIAE NADPH-CYTOCHROME P450 REDUCTASE Thesis submitted in accordance with the requirements of the University of Liverpool for the degree of Doctor in Philosophy by PHILIP WIDDOWSON SEPTEMBER 2010 0 ACKNOWLEDGEMENTS There are a number of people whom I would like to thank for their support during the completion of this thesis. Firstly, I would like to thank my family; Mum, Louise and Chris for putting up with me over the years and for their love, patience and, in particular to Chris, technical support throughout– I could not have coped on my own without all your help. I would like to extend special thanks to Professor Lu-Yun Lian for her constant supervision throughout my Ph.D. She always kept me on the right path and was always available for support and advice which was especially useful when things were not going to plan. Thank you for all your help. In addition to Professor Lian I would like to thank all the members of the Structural Biology Group and everybody, past and present, whom I worked alongside in Lab C over the past four years. I would also like to thank the University of Liverpool for the funding that made all this possible. I would like to make particular mention to a few people in the School of Biological Sciences who were of particular help during my time at university. Dr. Mark Wilkinson was a constant support, not only during my Ph.D, but as my undergraduate tutor and honours project supervisor. Dr. Dan Rigden and Dr. -
Single-Molecule Spectroscopy Reveals How Calmodulin Activates NO Synthase by Controlling Its Conformational Fluctuation Dynamics
Single-molecule spectroscopy reveals how calmodulin activates NO synthase by controlling its conformational fluctuation dynamics Yufan Hea,1, Mohammad Mahfuzul Haqueb,1, Dennis J. Stuehrb,2, and H. Peter Lua,2 aCenter for Photochemical Sciences, Department of Chemistry, Bowling Green State University, Bowling Green, OH 43403; and bDepartment of Pathobiology, Lerner Research Institute, Cleveland Clinic, Cleveland, OH 44195 Edited by Louis J. Ignarro, University of California, Los Angeles School of Medicine, Beverly Hills, CA, and approved July 31, 2015 (received for review May 5, 2015) Mechanisms that regulate the nitric oxide synthase enzymes (NOS) this model, the FMN domain is suggested to be highly dynamic are of interest in biology and medicine. Although NOS catalysis and flexible due to a connecting hinge that allows it to alternate relies on domain motions, and is activated by calmodulin binding, between its electron-accepting (FAD→FMN) or closed confor- the relationships are unclear. We used single-molecule fluores- mation and electron-donating (FMN→heme) or open conforma- cence resonance energy transfer (FRET) spectroscopy to elucidate tion (Fig. 1 A and B)(28,30–36). In the electron-accepting closed the conformational states distribution and associated conforma- conformation, the FMN domain interacts with the NADPH/FAD tional fluctuation dynamics of the two electron transfer domains domain (FNR domain) to receive electrons, whereas in the elec- in a FRET dye-labeled neuronal NOS reductase domain, and to tron donating open conformation the FMN domain has moved understand how calmodulin affects the dynamics to regulate away to expose the bound FMN cofactor so that it may transfer catalysis. -
View, the Catalytic Center of Bnoss Is Almost Identical to Mnos Except That a Conserved Val Near Heme Iron in Mnos Is Substituted by Iie[25]
STUDY OF ELECTRON TRANSFER THROUGH THE REDUCTASE DOMAIN OF NEURONAL NITRIC OXIDE SYNTHASE AND DEVELOPMENT OF BACTERIAL NITRIC OXIDE SYNTHASE INHIBITORS YUE DAI Bachelor of Science in Chemistry Wuhan University June 2008 submitted in partial fulfillment of requirements for the degree DOCTOR OF PHILOSOPHY IN CLINICAL AND BIOANALYTICAL CHEMISTRY at the CLEVELAND STATE UNIVERSITY July 2016 We hereby approve this dissertation for Yue Dai Candidate for the Doctor of Philosophy in Clinical-Bioanalytical Chemistry Degree for the Department of Chemistry and CLEVELAND STATE UNIVERSITY’S College of Graduate Studies by Dennis J. Stuehr. PhD. Department of Pathobiology, Cleveland Clinic / July 8th 2016 Mekki Bayachou. PhD. Department of Chemistry / July 8th 2016 Thomas M. McIntyre. PhD. Department of Cellular and Molecular Medicine, Cleveland Clinic / July 8th 2016 Bin Su. PhD. Department of Chemistry / July 8th 2016 Jun Qin. PhD. Department of Molecular Cardiology, Cleveland Clinic / July 8th 2016 Student’s Date of Defense: July 8th 2016 ACKNOWLEDGEMENT First I would like to express my special appreciation and thanks to my Ph. D. mentor, Dr. Dennis Stuehr. You have been a tremendous mentor for me. It is your constant patience, encouraging and support that guided me on the road of becoming a research scientist. Your advices on both research and life have been priceless for me. I would like to thank my committee members - Professor Mekki Bayachou, Professor Bin Su, Dr. Thomas McIntyre, Dr. Jun Qin and my previous committee members - Dr. Donald Jacobsen and Dr. Saurav Misra for sharing brilliant comments and suggestions with me. I would like to thank all our lab members for their help ever since I joint our lab. -
Precursor of Ether Phospholipids Is Synthesized by a Flavoenzyme
Precursor of ether phospholipids is synthesized by a flavoenzyme through covalent catalysis Simone Nencia, Valentina Pianoa, Sara Rosatib, Alessandro Alivertic, Vittorio Pandinic, Marco W. Fraaijed, Albert J. R. Heckb, Dale E. Edmondsone, and Andrea Mattevia,1 aDepartment of Biology and Biotechnology, University of Pavia, 27100 Pavia, Italy; bBiomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University and Netherlands Proteomics Centre, 3584 CH Utrecht, The Netherlands; cDepartment of Biosciences, University of Milan, 20133 Milan, Italy; dMolecular Enzymology Group, University of Groningen, 9747 AG Groningen, The Netherlands; and eDepartment of Biochemistry, Emory University, Atlanta, GA 30322 Edited by Emil F. Pai, Ontario Cancer Institute/Princess Margaret Hospital, Toronto, ON, Canada, and accepted by the Editorial Board October 5, 2012 (received for review August 31, 2012) The precursor of the essential ether phospholipids is synthesized ADPS enzymes, whereas type 1 arises from mutations in PEX7, by a peroxisomal enzyme that uses a flavin cofactor to catalyze the protein mediating the peroxisomal import of ADPS (9–12). a reaction that does not alter the redox state of the substrates. Here we report a structural and mechanistic investigation of The enzyme crystal structure reveals a V-shaped active site with mammalian ADPS in WT and mutated forms. The biochemical a narrow constriction in front of the prosthetic group. Mutations hallmark of the enzyme is that it uses a redox cofactor, flavin causing inborn ether phospholipid deficiency, a very severe adenine dinucleotide (FAD), to catalyze a reaction that does not genetic disease, target residues that are part of the catalytic alter the redox state of the substrates (10, 13). -
2010 Physical Biosciences Research Meeting
2010 Physical Biosciences Research Meeting Sheraton Inner Harbor Hotel Baltimore, MD October 17-20, 2010 Office of Basic Energy Sciences Chemical Sciences, Geosciences & Biosciences Division 2010 Physical Biosciences Research Meeting Program and Abstracts Sheraton Inner Harbor Hotel Baltimore, MD October 17-20, 2010 Chemical Sciences, Geosciences, and Biosciences Division Office of Basic Energy Sciences Office of Science U.S. Department of Energy i Cover art is taken from the public domain and can be found at: http://commons.wikimedia.org/wiki/File:Blue_crab_on_market_in_Piraeus_-_Callinectes_sapidus_Rathbun_20020819- 317.jpg This document was produced under contract number DE-AC05-060R23100 between the U.S. Department of Energy and Oak Ridge Associated Universities. The research grants and contracts described in this document are, unless specifically labeled otherwise, supported by the U.S. DOE Office of Science, Office of Basic Energy Sciences, Chemical Sciences, Geosciences, and Biosciences Division. ii Foreword This volume provides a record of the 2nd biennial meeting of the Principal Investigators (PIs) funded by the Physical Biosciences program, and is sponsored by the Chemical Sciences, Geosciences, and Biosciences Division of the Office of Basic Energy Sciences (BES) in the U.S. Department of Energy (DOE). Within DOE-BES there are two programs that fund basic research in energy-relevant biological sciences, Physical Biosciences and Photosynthetic Systems. These two Biosciences programs, along with a strong program in Solar Photochemistry, comprise the current Photo- and Bio- Chemistry Team. This meeting specifically brings together under one roof all of the PIs funded by the Physical Biosciences program, along with Program Managers and staff not only from DOE-BES, but also other offices within DOE, the national labs, and even other federal funding agencies. -
Cbic.202000100Taverne
Delft University of Technology A Minimized Chemoenzymatic Cascade for Bacterial Luciferase in Bioreporter Applications Phonbuppha, Jittima; Tinikul, Ruchanok; Wongnate, Thanyaporn; Intasian, Pattarawan; Hollmann, Frank; Paul, Caroline E.; Chaiyen, Pimchai DOI 10.1002/cbic.202000100 Publication date 2020 Document Version Final published version Published in ChemBioChem Citation (APA) Phonbuppha, J., Tinikul, R., Wongnate, T., Intasian, P., Hollmann, F., Paul, C. E., & Chaiyen, P. (2020). A Minimized Chemoenzymatic Cascade for Bacterial Luciferase in Bioreporter Applications. ChemBioChem, 21(14), 2073-2079. https://doi.org/10.1002/cbic.202000100 Important note To cite this publication, please use the final published version (if applicable). Please check the document version above. Copyright Other than for strictly personal use, it is not permitted to download, forward or 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 such as Creative Commons. Takedown policy Please contact us and provide details if you believe this document breaches copyrights. We will remove access to the work immediately and investigate your claim. This work is downloaded from Delft University of Technology. For technical reasons the number of authors shown on this cover page is limited to a maximum of 10. Green Open Access added to TU Delft Institutional Repository ‘You share, we take care!’ – Taverne project https://www.openaccess.nl/en/you-share-we-take-care Otherwise as indicated in the copyright section: the publisher is the copyright holder of this work and the author uses the Dutch legislation to make this work public. -
Supplementary Materials
Supplementary Materials COMPARATIVE ANALYSIS OF THE TRANSCRIPTOME, PROTEOME AND miRNA PROFILE OF KUPFFER CELLS AND MONOCYTES Andrey Elchaninov1,3*, Anastasiya Lokhonina1,3, Maria Nikitina2, Polina Vishnyakova1,3, Andrey Makarov1, Irina Arutyunyan1, Anastasiya Poltavets1, Evgeniya Kananykhina2, Sergey Kovalchuk4, Evgeny Karpulevich5,6, Galina Bolshakova2, Gennady Sukhikh1, Timur Fatkhudinov2,3 1 Laboratory of Regenerative Medicine, National Medical Research Center for Obstetrics, Gynecology and Perinatology Named after Academician V.I. Kulakov of Ministry of Healthcare of Russian Federation, Moscow, Russia 2 Laboratory of Growth and Development, Scientific Research Institute of Human Morphology, Moscow, Russia 3 Histology Department, Medical Institute, Peoples' Friendship University of Russia, Moscow, Russia 4 Laboratory of Bioinformatic methods for Combinatorial Chemistry and Biology, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Moscow, Russia 5 Information Systems Department, Ivannikov Institute for System Programming of the Russian Academy of Sciences, Moscow, Russia 6 Genome Engineering Laboratory, Moscow Institute of Physics and Technology, Dolgoprudny, Moscow Region, Russia Figure S1. Flow cytometry analysis of unsorted blood sample. Representative forward, side scattering and histogram are shown. The proportions of negative cells were determined in relation to the isotype controls. The percentages of positive cells are indicated. The blue curve corresponds to the isotype control. Figure S2. Flow cytometry analysis of unsorted liver stromal cells. Representative forward, side scattering and histogram are shown. The proportions of negative cells were determined in relation to the isotype controls. The percentages of positive cells are indicated. The blue curve corresponds to the isotype control. Figure S3. MiRNAs expression analysis in monocytes and Kupffer cells. Full-length of heatmaps are presented. -
Structural Features That Promote Catalysis in Two-Component Systems Involved in Sulfur Metabolism
Structural Features That Promote Catalysis in Two-Component Systems Involved in Sulfur Metabolism by Richard Allen Hagen A dissertation to the Graduate Faculty of Auburn University in partial fulfillment of the requirements for the Degree of Doctor of Philosophy Auburn, Alabama August 8, 2020 Copyright 2020 by Richard Allen Hagen Approved by Holly R. Ellis, Chair, Professor of Chemistry and Biochemistry Douglas C. Goodwin, Professor of Chemistry and Biochemistry Evert C. Duin, Professor of Chemistry and Biochemistry Steven Mansoorabadi, Associate Professor of Chemistry and Biochemistry Abstract Sulfur is an essential element important in the synthesis of biomolecules. Bacteria are able to assimilate inorganic sulfur for the biosynthesis of L-cysteine. Inorganic sulfate is often unavailable, so bacteria have evolved multiple metabolic pathways to obtain sulfur from alternative sources. Interestingly, many of the enzymes involved in sulfur acquisition are flavin- dependent two-component systems. These two-component systems consist of a flavin reductase and monooxygenase that utilize flavin to cleave the carbon-sulfur bonds of organosulfur compounds. The two-component systems differ in their characterized sulfur substrate specificity. Enzymes SsuE/SsuD are involved in the desulfonation of linear alkanesulfonates (C2-C10), enzymes MsuE/MsuD utilize methanesulfonate (C1), and enzymes SfnF/SfnG utilize DMSO2 as a sulfur source. The flavin reductases involved in sulfur assimilation utilize FMN as a substrate but differ in their ability to utilize NADH or NADPH. The alkanesulfonate monooxygenase system was the first two-component flavin-dependent system expressed during sulfur limiting conditions that was characterized. The flavin reductase (SsuE) and monooxygenase (SsuD) have distinct structural and functional properties, but the two enzymes must synchronize their functions for catalysis to occur. -
On the Natural History of Flavin-Based Electron Bifurcation
On the Natural History of Flavin-Based Electron Bifurcation Frauke Baymann, Barbara Schoepp-Cothenet, Simon Duval, Marianne Guiral, Myriam Brugna, Carole Baffert, Michael Russell, Wolfgang Nitschke To cite this version: Frauke Baymann, Barbara Schoepp-Cothenet, Simon Duval, Marianne Guiral, Myriam Brugna, et al.. On the Natural History of Flavin-Based Electron Bifurcation. Frontiers in Microbiology, Frontiers Media, 2018, 9, pp.1357 - 1357. 10.3389/fmicb.2018.01357. hal-01828959 HAL Id: hal-01828959 https://hal-amu.archives-ouvertes.fr/hal-01828959 Submitted on 5 Jul 2018 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. fmicb-09-01357 June 29, 2018 Time: 19:12 # 1 REVIEW published: 03 July 2018 doi: 10.3389/fmicb.2018.01357 On the Natural History of Flavin-Based Electron Bifurcation Frauke Baymann1, Barbara Schoepp-Cothenet1, Simon Duval1, Marianne Guiral1, Myriam Brugna1, Carole Baffert1, Michael J. Russell2 and Wolfgang Nitschke1* 1 CNRS, BIP, UMR 7281, IMM FR3479, Aix-Marseille University, Marseille, France, 2 Jet Propulsion Laboratory, California Institute of Technology, Pasadena, CA, United States Electron bifurcation is here described as a special case of the continuum of electron transfer reactions accessible to two-electron redox compounds with redox cooperativity. -
Biochemical Characterization of 2-Nitropropane Dioxygenase from Hansenula MRAKII
Georgia State University ScholarWorks @ Georgia State University Chemistry Theses Department of Chemistry 4-22-2008 Biochemical Characterization of 2-Nitropropane Dioxygenase from Hansenula MRAKII Slavica Mijatovic Follow this and additional works at: https://scholarworks.gsu.edu/chemistry_theses Recommended Citation Mijatovic, Slavica, "Biochemical Characterization of 2-Nitropropane Dioxygenase from Hansenula MRAKII." Thesis, Georgia State University, 2008. https://scholarworks.gsu.edu/chemistry_theses/8 This Thesis is brought to you for free and open access by the Department of Chemistry at ScholarWorks @ Georgia State University. It has been accepted for inclusion in Chemistry Theses by an authorized administrator of ScholarWorks @ Georgia State University. For more information, please contact [email protected]. BIOCHEMICAL CHARACTERIZATION OF 2-NITROPROPANE DIOXYGENASE FROM HANSENULA MRAKII by SLAVICA MIJATOVIC Under the Direction of Dr. Giovanni Gadda ABSTRACT 2-Nitropropane dioxygenase from Hansenula mrakii is a flavin-dependent enzyme that catalyzes the oxidation of anionic nitroalkanes into the corresponding carbonyl compounds and nitrite, with oxygen as the electron acceptor. Although nitroalkanes are anticipated to be toxic and carcinogenic, they are used widely in chemical industry for a quick and effective way of synthesizing common reagents. Consequently, the biochemical and biophysical analysis of 2- nitropropane dioxyganase has a potential for bioremediation purposes. In this study, recombinant enzyme is purified to high levels, allowing for detailed characterization. The biochemical analysis of 2-nitropropane dioxygenase presented in this study has established that enzyme utilizes alkyl nitronates as substrates by forming an anionic flavosemiquinone in catalysis. The enzyme is inhibited by halide ions, does not contain iron and has a positive charge located close to the N(1)-C(2)=O locus of the isoalloxazine moiety of the FMN cofactor. -
Thermostable Flavin Reductase That Couples with Dibenzothiophene Monooxygenase, from Thermophilic Bacillus Sp
Biosci. Biotechnol. Biochem., 68 (8), 1712–1721, 2004 Thermostable Flavin Reductase That Couples with Dibenzothiophene Monooxygenase, from Thermophilic Bacillus sp. DSM411: Purification, Characterization, and Gene Cloning Takashi OHSHIRO, Hiroko YAMADA, Tomohisa SHIMODA, y Toshiyuki MATSUBARA, and Yoshikazu IZUMI Department of Biotechnology, Tottori University, Tottori 680-8552, Japan Received April 5, 2004; Accepted June 1, 2004 Flavin reductase is essential for the oxygenases enzyme from V. fischeri has been determined.13) In involved in microbial dibenzothiophene (DBT) desul- addition, multiple flavin reductases were found in furization. An enzyme of the thermophilic strain, Escherichia coli and Bacillus subtilis, and some of Bacillus sp. DSM411, was selected to couple with DBT them were shown to have nitroreductase activity monooxygenase (DszC) from Rhodococcus erythropolis catalyzing the reduction of aromatic nitrocompounds D-1. The flavin reductase was purified to homogeneity other than flavin compounds.14–16) The crystal structures from Bacillus sp. DSM411, and the native enzyme was a of the enzymes from E. coli have been solved.17,18) monomer of Mr 16 kDa. Although the best substrates We have studied microbial dibenzothiophene (DBT) were flavin mononucleotide and NADH, the enzyme also desulfurization in its enzymological and molecular used other flavin compounds and acted slightly on biological aspects.19,20) The sulfur-specific metabolic nitroaromatic compounds and NADPH. The purified pathway of DBT was investigated using two mesophilic enzyme coupled with DszC and had a ferric reductase Rhodococcus strains, R. erythropolis IGTS8 and activity. Among the flavin reductases so far character- R. erythropolis D-1.19,20) DBT was initially oxidized ized, the present enzyme is the most thermophilic and by two monooxygenases, DBT monooxygenase (DszC) thermostable.