Microbially Mediated Transformation of Dissolved Nitrogen in Aquatic Environments a Dissertation Submitted to Kent State Univers
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Novel Copper-Containing Membrane Monooxygenases (Cummos) Encoded by Alkane- Utilizing Betaproteobacteria
Lawrence Berkeley National Laboratory Recent Work Title Novel copper-containing membrane monooxygenases (CuMMOs) encoded by alkane- utilizing Betaproteobacteria. Permalink https://escholarship.org/uc/item/8z48x96q Journal The ISME journal, 14(3) ISSN 1751-7362 Authors Rochman, Fauziah F Kwon, Miye Khadka, Roshan et al. Publication Date 2020-03-01 DOI 10.1038/s41396-019-0561-2 Peer reviewed eScholarship.org Powered by the California Digital Library University of California 1 1 2 1Novel copper-containing membrane monooxygenases 2(CuMMOs) encoded by alkane-utilizing Betaproteobacteria 3 4Running title: Novel CuMMOs in Betaproteobacteria 5 6Fauziah F. Rochman1, Miye Kwon2, Roshan Khadka1, Ivica Tamas1,3, Azriel 7Abraham Lopez-Jauregui1,4, Andriy Sheremet1, Angela Smirnova1, Rex R. 8Malmstrom5, Sukhwan Yoon2, Tanja Woyke5, Peter F. Dunfield1*, Tobin J. 9Verbeke1 10 111 Department of Biological Sciences, University of Calgary, 2500 University 12Dr. NW Calgary AB Canada T2N 1N4 132 Department of Civil and Environmental Engineering, Korea Advanced 14Institute of Science and Technology, Daejeon, Korea 153Department of Biology and Ecology, University of Novi Sad Novi Sad, Serbia 164 Instituto Tecnologico y de Estudios Superiores de Monterrey, Chihuahua, 17Mexico 185 Department of Energy Joint Genome Institute, Walnut Creek, California, 19USA. 20 21*Corresponding author: [email protected]; 403-220-2469 22 3 2 4 23Competing interests: The authors declare that they have no competing 24interests. 5 3 6 25Abstract 26Copper-containing membrane monooxygenases (CuMMOs) are encoded by 27xmoCAB(D) gene clusters and catalyze the oxidation of methane, ammonia, 28or some short chain alkanes and alkenes. In a metagenome constructed from 29an oilsands tailings pond we detected an xmoCABD gene cluster with <59% 30derived amino acid identity to genes from known bacteria. -
ORGANIC GEOCHEMISTRY: CHALLENGES for the 21St CENTURY
ORGANIC GEOCHEMISTRY: CHALLENGES FOR THE 21st CENTURY VOL. 2 Book of Abstracts of the Communications presented to the 22nd International Meeting on Organic Geochemistry Seville – Spain. September 12 -16, 2005 Editors: F.J. González-Vila, J.A. González-Pérez and G. Almendros Equipo de trabajo: Rocío González Vázquez Antonio Terán Rodíguez José Mª de la Rosa Arranz Maquetación: Rocío González Vázquez Fotomecánica e impresión: Akron Gráfica, Sevilla © 22nd IMOG, Sevilla 2005 Depósito legal: SE-61181-2005 I.S.B.N.: 84-689-3661-8 COMMITTEES INVOLVED IN THE ORGANIZATION OF THE 22 IMOG 2005 Chairman: Francisco J. GONZÁLEZ-VILA Vice-Chairman: José A. GONZÁLEZ-PÉREZ Consejo Superior de Investigaciones Científicas (CSIC) Instituto de Recursos Naturales y Agrobiología de Sevilla (IRNAS) Scientific Committee Francisco J. GONZÁLEZ-VILA (Chairman) IRNAS-CSIC, Spain Gonzalo ALMENDROS Claude LARGEAU CCMA-CSIC, Spain ENSC, France Pim van BERGEN José C. del RÍO SHELL Global Solutions, The Netherlands IRNAS-CSIC, Spain Jørgen A. BOJESEN-KOEFOED Jürgen RULLKÖTTER GEUS, Denmark ICBM, Germany Chris CORNFORD Stefan SCHOUTEN IGI, UK NIOZ, The Netherlands Gary ISAKSEN Eugenio VAZ dos SANTOS NETO EXXONMOBIL, USA PETROBRAS RD, Brazil Local Committee José Ramón de ANDRÉS IGME, Spain Mª Carmen DORRONSORO Mª Enriqueta ARIAS Universidad del País Vasco Universidad de Alcalá Antonio GUERRERO Tomasz BOSKI Universidad de Sevilla Universidad do Algarve, Faro, Portugal Juan LLAMAS Ignacio BRISSON ETSI Minas de Madrid Repsol YPF Albert PERMANYER Juan COTA Universidad de Barcelona Universidad de Sevilla EAOG Board Richard L. PATIENCE (Chairman) Sylvie DERENNE (Secretary) Ger W. van GRAAS (Treasurer) Walter MICHAELIS (Awards) Francisco J. GONZALEZ-VILA (Newsletter) C. -
Histamine Degradation by Halophilic Archaea Wanaporn Tapingkae A
Histamine Degradation by Halophilic Archaea Wanaporn Tapingkae A Thesis Submitted in Partial Fulfillment of the Requirements for the Degree of Doctor of Philosophy in Food Technology Prince of Songkla University 2009 Copyright of Prince of Songkla University i Thesis Title Histamine Degradation by Halophilic Archaea Author Miss Wanaporn Tapingkae Major Program Food Technology Major Advisor Examining Committee : ……..…………………………………. ……..…………..…………….Chairperson (Dr. Wonnop Visessanguan) (Asst. Prof. Dr. Tipparat Hongpattarakere) ……..…………………..……………….… Co-advisors (Dr. Wonnop Visessanguan) ……..…………………………………. ……..…………………..……………….… (Prof. Dr. Soottawat Benjakul) (Prof. Dr. Soottawat Benjakul) ……..…………………………………. ……..…………………..……………….… (Prof. Dr. Kirk L. Parkin) (Assoc. Prof. Dr. Somboon Tanasupawat) ……..…………………..……………….… (Assoc. Prof. Dr. Borwonsak Leenanon) The Graduate School, Prince of Songkla University, has approved this thesis as partial fulfillment of the requirements for the Doctor of Philosophy Degree in Food Technology ………………………………………… (Assoc. Prof. Dr. Krerkchai Thongnoo) Dean of Graduate School ii ชือวทยานิ ิพนธ์ การยอยสลายฮ่ ีสตามีนโดยอาเคียที่ชอบเกลือ ผู้เขียน นางสาววรรณพร ทะพิงคแก์ สาขาวชาิ เทคโนโลยอาหารี ปี การศึกษา 2551 บทคดยั ่อ ปริมาณฮีสตามีนที่สูงก่อใหเก้ ิดผลเสียหายต่อทงคั ุณภาพและความปลอดภยของั นาปลาํ ดงนั นการทดลองนั ีจึงมีวตถั ุประสงคเพ์ ื่อคดแยกเชั ืออาเคียที่ชอบเกลือที่มีความสามารถยอย่ ฮีสตามีนในสภาวะที่มีเกลือสูง ศึกษาเอนไซมท์ ี่เกี่ยวของ้ และศึกษาความเป็นไปไดในการประย้ กตุ ์ ใชในกระบวนการผล้ ิตนาปลาํ จากเชืออาเคียที่ชอบเกลือ -
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, . -
Hyperbilirubinemia
Porphyrins Porphyrins (Porphins) are cyclic tetrapyrol compounds formed by the linkage )). of four pyrrole rings through methenyl bridges (( HC In the reduced porphyrins (Porphyrinogens) the linkage of four pyrrole rings (tetrapyrol) through methylene bridges (( CH2 )) The characteristic property of porphyrins is the formation of complexes with the metal ion bound to nitrogen atoms of the pyrrole rings. e.g. Heme (iron porphyrin). Proteins which contain heme ((hemoproteins)) are widely distributed e.g. Hemoglobin, Myoglobin, Cytochromes, Catalase & Tryptophan pyrrolase. Natural porphyrins have substituent side chains on the eight hydrogen atoms numbered on the pyrrole rings. These side chains are: CH 1-Methyl-group (M)… (( 3 )) 2-Acetate-group (A)… (( CH2COOH )) 3-Propionate-group (P)… (( CH2CH2COOH )) 4-Vinyl-group (V)… (( CH CH2 )) Porphyrins with asymmetric arrangement of the side chains are classified as type III porphyrins while those with symmetric arrangement of the side chains are classified as type I porphyrins. Only types I & III are present in nature & type III series is more important because it includes heme. 1 Heme Biosynthesis Heme biosynthesis occurs through the following steps: 1-The starting reaction is the condensation between succinyl-CoA ((derived from citric acid cycle in the mitochondria)) & glycine, this reaction is a rate limiting reaction in the hepatic heme synthesis, it occurs in the mitochondria & is catalyzed by ALA synthase (Aminolevulinate synthase) enzyme in the presence of pyridoxal phosphate as a cofactor. The product of this reaction is α-amino-β-ketoadipate which is rapidly decarboxylated to form δ-aminolevulinate (ALA). 2-In the cytoplasm condensation reaction between two molecules of ALA is catalyzed by ALA dehydratase enzyme to form two molecules of water & one 2 molecule of porphobilinogen (PBG) which is a precursor of pyrrole. -
Thermophilic Lithotrophy and Phototrophy in an Intertidal, Iron-Rich, Geothermal Spring 2 3 Lewis M
bioRxiv preprint doi: https://doi.org/10.1101/428698; this version posted September 27, 2018. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. 1 Thermophilic Lithotrophy and Phototrophy in an Intertidal, Iron-rich, Geothermal Spring 2 3 Lewis M. Ward1,2,3*, Airi Idei4, Mayuko Nakagawa2,5, Yuichiro Ueno2,5,6, Woodward W. 4 Fischer3, Shawn E. McGlynn2* 5 6 1. Department of Earth and Planetary Sciences, Harvard University, Cambridge, MA 02138 USA 7 2. Earth-Life Science Institute, Tokyo Institute of Technology, Meguro, Tokyo, 152-8550, Japan 8 3. Division of Geological and Planetary Sciences, California Institute of Technology, Pasadena, CA 9 91125 USA 10 4. Department of Biological Sciences, Tokyo Metropolitan University, Hachioji, Tokyo 192-0397, 11 Japan 12 5. Department of Earth and Planetary Sciences, Tokyo Institute of Technology, Meguro, Tokyo, 13 152-8551, Japan 14 6. Department of Subsurface Geobiological Analysis and Research, Japan Agency for Marine-Earth 15 Science and Technology, Natsushima-cho, Yokosuka 237-0061, Japan 16 Correspondence: [email protected] or [email protected] 17 18 Abstract 19 Hydrothermal systems, including terrestrial hot springs, contain diverse and systematic 20 arrays of geochemical conditions that vary over short spatial scales due to progressive interaction 21 between the reducing hydrothermal fluids, the oxygenated atmosphere, and in some cases 22 seawater. At Jinata Onsen, on Shikinejima Island, Japan, an intertidal, anoxic, iron- and 23 hydrogen-rich hot spring mixes with the oxygenated atmosphere and sulfate-rich seawater over 24 short spatial scales, creating an enormous range of redox environments over a distance ~10 m. -
RLIN1, Encoding a Putative Coproporphyrinogen III Oxidase, Is Involved in Lesion Initiation in Rice
Available online at www.sciencedirect.com Journal of Genetics and Genomics 38 (2011) 29e37 www.jgenetgenomics.org RLIN1, encoding a putative coproporphyrinogen III oxidase, is involved in lesion initiation in rice Changhui Sun a,b,d,1, Linchuan Liu b,c,1, Jiuyou Tang b, Aihong Lin b,c, Fantao Zhang b,d, Jun Fang b, Genfa Zhang a,*, Chengcai Chu a,b,c,* a Key Laboratory for Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Science, Beijing Normal University, Beijing 100875, China b The State Key Laboratory of Plant Genomics and National Plant Gene Research Center (Beijing), Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Datun Road, Chaoyang District, Beijing 100101, China c Graduate School of the Chinese Academy of Sciences, Yuquan Road, Beijing 100039, China d Rice Research Institute, Sichuan Agricultural University, Chengdu 611130, China Received 11 October 2010; revised 17 October 2010; accepted 20 October 2010 Abstract Lesion mimic is necrotic lesions on plant leaf or stem in the absence of pathogenic infection, and its exact biological mechanism is varied. By a large-scale screening of our T-DNA mutant population, we identified a mutant rice lesion initiation 1 (rlin1), which was controlled by a single nuclear recessive gene. Map-based cloning revealed that RLIN1 encoded a putative coproporphyrinogen III oxidase in tetrapyrrole biosynthesis pathway. Sequencing results showed that a G to T substitution occurred in the second exon of RLIN1 and led to a missense mutation from Asp to Tyr. Ectopic expression of RLIN1 could rescue rlin1 lesion mimic phenotype. -
Porphyrins & Bile Pigments
Bio. 2. ASPU. Lectu.6. Prof. Dr. F. ALQuobaili Porphyrins & Bile Pigments • Biomedical Importance These topics are closely related, because heme is synthesized from porphyrins and iron, and the products of degradation of heme are the bile pigments and iron. Knowledge of the biochemistry of the porphyrins and of heme is basic to understanding the varied functions of hemoproteins in the body. The porphyrias are a group of diseases caused by abnormalities in the pathway of biosynthesis of the various porphyrins. A much more prevalent clinical condition is jaundice, due to elevation of bilirubin in the plasma, due to overproduction of bilirubin or to failure of its excretion and is seen in numerous diseases ranging from hemolytic anemias to viral hepatitis and to cancer of the pancreas. • Metalloporphyrins & Hemoproteins Are Important in Nature Porphyrins are cyclic compounds formed by the linkage of four pyrrole rings through methyne (==HC—) bridges. A characteristic property of the porphyrins is the formation of complexes with metal ions bound to the nitrogen atom of the pyrrole rings. Examples are the iron porphyrins such as heme of hemoglobin and the magnesium‐containing porphyrin chlorophyll, the photosynthetic pigment of plants. • Natural Porphyrins Have Substituent Side Chains on the Porphin Nucleus The porphyrins found in nature are compounds in which various side chains are substituted for the eight hydrogen atoms numbered in the porphyrin nucleus. As a simple means of showing these substitutions, Fischer proposed a shorthand formula in which the methyne bridges are omitted and a porphyrin with this type of asymmetric substitution is classified as a type III porphyrin. -
Noncanonical Coproporphyrin-Dependent Bacterial Heme Biosynthesis Pathway That Does Not Use Protoporphyrin
Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin Harry A. Daileya,b,c,1, Svetlana Gerdesd, Tamara A. Daileya,b,c, Joseph S. Burcha, and John D. Phillipse aBiomedical and Health Sciences Institute and Departments of bMicrobiology and cBiochemistry and Molecular Biology, University of Georgia, Athens, GA 30602; dMathematics and Computer Science Division, Argonne National Laboratory, Argonne, IL 60439; and eDivision of Hematology, Department of Medicine, University of Utah School of Medicine, Salt Lake City, UT 84132 Edited by J. Clark Lagarias, University of California, Davis, CA, and approved January 12, 2015 (received for review August 25, 2014) It has been generally accepted that biosynthesis of protoheme of a “primitive” pathway in Desulfovibrio vulgaris (13). This path- (heme) uses a common set of core metabolic intermediates that way, named the “alternative heme biosynthesis” path (or ahb), has includes protoporphyrin. Herein, we show that the Actinobacteria now been characterized by Warren and coworkers (15) in sulfate- and Firmicutes (high-GC and low-GC Gram-positive bacteria) are reducing bacteria. In the ahb pathway, siroheme, synthesized unable to synthesize protoporphyrin. Instead, they oxidize copro- from uroporphyrinogen III, can be further metabolized by suc- porphyrinogen to coproporphyrin, insert ferrous iron to make Fe- cessive demethylation and decarboxylation to yield protoheme (14, coproporphyrin (coproheme), and then decarboxylate coproheme 15) (Fig. 1 and Fig. S1). A similar pathway exists for protoheme- to generate protoheme. This pathway is specified by three genes containing archaea (15, 16). named hemY, hemH, and hemQ. The analysis of 982 representa- Current gene annotations suggest that all enzymes for pro- tive prokaryotic genomes is consistent with this pathway being karyotic heme synthetic pathways are now identified. -
Nicole Kube Phd
Leibniz-Institut für Meereswissenschaften The integration of microalgae photobioreactors in a recirculation system for low water discharge mariculture Dissertation zur Erlangung des Doktorgrades der Mathematisch-Naturwissenschaftlichen Fakultät an der Christian-Albrechts-Universität zu Kiel vorgelegt von Nicole Kube Kiel, 2006 Referentin: Prof. Dr. Karin Lochte Koreferent: Prof. Dr. Dr. h.c. Harald Rosenthal Tag der mündlichen Prüfung: Zum Druck genehmigt: Kiel, den Der Dekan Foreword The manuscripts included in this thesis are prepared for submission to peer- reviewed journals as listed below: Wecker B., Kube N., Bischoff A.A., Waller U. (2006). MARE – Marine Artificial Recirculated Ecosystem: feasibility and modelling of a novel integrated recirculation system. (manuscript) Kube N., Bischoff A.A., Wecker B., Waller U. Cultivation of microalgae using a continuous photobioreactor system based on dissolved nutrients of a recirculation system for low water discharge mariculture (manuscript) Kube N. And Rosenthal H. Ozonation and foam fractionation used for the removal of bacteria and parti- cles in a marine recirculation system for microalgae cultivation (manuscript) Kube N., Bischoff A.A., Blümel M., Wecker B., Waller U. MARE – Marine Artificial Recirulated Ecosystem II: Influence on the nitrogen cycle in a marine recirculation system with low water discharge by cultivat- ing detritivorous organisms and phototrophic microalgae. (manuscript) This thesis has been realised with the help of several collegues. The contributions in particular -
Functional Characterization of Seven Γ-Glutamylpolyamine Synthetase
JOURNAL OF BACTERIOLOGY, Aug. 2011, p. 3923–3930 Vol. 193, No. 15 0021-9193/11/$12.00 doi:10.1128/JB.05105-11 Copyright © 2011, American Society for Microbiology. All Rights Reserved. Functional Characterization of Seven ␥-Glutamylpolyamine Synthetase Genes and the bauRABCD Locus for Polyamine and -Alanine Utilization in Pseudomonas aeruginosa PAO1ᰔ Xiangyu Yao,1† Weiqing He,1,2† and Chung-Dar Lu1,3* Department of Biology, Georgia State University, Atlanta, Georgia 303031; Institute of Medicinal Biotechnology, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 100050, China2; and Department of Medical Laboratory Sciences and Biotechnology, China Medical University, Taichung, Taiwan 404023 Received 16 April 2011/Accepted 13 May 2011 Pseudomonas aeruginosa and many other bacteria can utilize biogenic polyamines, including diaminopropane (DAP), putrescine (Put), cadaverine (Cad), and spermidine (Spd), as carbon and/or nitrogen sources. Tran- scriptome analysis in response to exogenous Put and Spd led to the identification of a list of genes encoding putative enzymes for the catabolism of polyamines. Among them, pauA1 to pauA6, pauB1 to pauB4, pauC, and pauD1 and pauD2 (polyamine utilization) encode enzymes homologous to Escherichia coli PuuABCD of the ␥-glutamylation pathway in converting Put into GABA. A series of unmarked pauA mutants was constructed for growth phenotype analysis. The results revealed that it requires specific combinations of pauA knockouts to abolish utilization of different polyamines and support the importance of ␥-glutamylation for polyamine catabolism in P. aeruginosa. Another finding was that the list of Spd-inducible genes overlaps almost completely with that of Put-inducible ones except the pauA3B2 operon and the bauABCD operon (-alanine utilization). -
Structural, Spectroscopic, and Mechanistic Insights Into the Three Phases of Nitrification Metallobiochemistry
STRUCTURAL, SPECTROSCOPIC, AND MECHANISTIC INSIGHTS INTO THE THREE PHASES OF NITRIFICATION METALLOBIOCHEMISTRY A Dissertation Presented to the Faculty of the Graduate School of Cornell University In Partial Fulfillment of the Requirements for the Degree of Doctor of Philosophy | Chemistry and Chemical Biology By Meghan Anne Smith August 2018 © 2018 Meghan Anne Smith STRUCTURAL, SPECTROSCOPIC, AND MECHANISTIC INSIGHTS INTO THE THREE PHASES OF NITRIFICATION METALLOBIOCHEMISTRY Meghan Anne Smith, Ph. D. Cornell University 2018 Biological ammonia (NH3) oxidation, referred to as nitrification, is a critical part of the biogeochemical nitrogen cycle. Nitrification is mediated by both bacteria and – archaea to ultimately oxidize NH3 to nitrite (NO 2 ), though there are also complete NH3-oxidizing (comammox) bacteria capable of oxidizing NH3 completely to nitrate – (NO3 ). In addition to these products, nitrification is also a major source of the by- products and environmental pollutants nitric oxide (NO), nitrous oxide (N2O) and nitrogen dioxide (NO2). Many steps of biological nitrification, including those leading to the production of these harmful products, are not currently clear; however, the work presented in this dissertation describes recent efforts and discoveries towards a complete understanding of the nitrification pathway. This process begins in both bacteria and archaea with the enzyme ammonia monooxygenase (AMO), which oxidizes NH3 to hydroxylamine (NH2OH). There exist two metal-binding sites in AMO of interest as these are highly conserved in AMOs and related enzymes. The true active site of this enzyme remains in debate, but here we show that both sites must remain intact for effective catalysis. In bacteria, the formed NH2OH is further oxidized to NO by the enzyme NH2OH oxidoreductase (HAO), though prior convention stated – that HAO was able to oxidize NH2OH fully to NO2 .