Α-Helical Segment 190 Α-Ketobutyrate 613 Α-Proteobacteria 780, 791 Α/Β

Total Page:16

File Type:pdf, Size:1020Kb

Α-Helical Segment 190 Α-Ketobutyrate 613 Α-Proteobacteria 780, 791 Α/Β Index A acyltransferase 123 adduct formation 815, 822 α-helical segment 190 adenosine-5´-phosphosulfate (APS) 610, 613 α-ketobutyrate 613 adenosine-5´-phosphosulfate reductase 610, 611 α-Proteobacteria 780, 791 adenosyl-GDP-cobinamide 91 α/β heterodimer 137–139 adenosyl cobalamin 72, 73, 82, 91 α helix 511 adenosylcobinamide phosphate 91 α polypeptide 175, 188, 204 adenosylcobyric acid 90 αβ LH1 subunit 513 adenylylsulfate 610, 613 A-branch 301 adenylysulfate:phosphate adenylyltransferase (APAT) 610 A-side electron transfer 346 Adiantum capillus-veneris 814 aa3-type cytochrome c oxidase 407, 408, 541, 636, 788 AdoMet:diacylglycerol 3-amino-3-carboxypropyl transferase AAA+ 69, 748 128 AAA+ ATPases 749 ADP-inhibition 477 AAA proteins 69 ADP sulfurylase 610 AAA+ proteins 70 Aequoria victoria 845 AAnP. See aerobic anoxygenic phototrophs aerobic anoxygenic phototrophs 19, 31, 32–52, 599 AAP. See aerobic anoxygenic phototrophs carbon metabolism 40–41 ABC. See ATP-binding cassette (ABC) deep ocean absorbance spectra vertical distribution 50 in vivo 39 ecological roles 47–51 absorption maxima 431 environment 32 carotenoid 926 evolution 38–40 absorption transitions 200 marine 48–49 accA 122 morphology 35 accB 122 nutritional status 43 accC 122 phylogeny 33, 37 accD 122 taxonomy 37 acceptor pool 530 aerobic bacteria 112 acceptor quinone 379, 380–399 aerobic cobalamin biosynthetic pathway 84 reactions 382 aerobic conditions 58, 72, 112, 417 acceptor quinone complex 383 aerobic cyclization system 72 accessory phototrophy 50 aerobic pathway 84 Acetobacteraceae 603, 614 aerobic photosynthetic bacteria 98, 99, 112 3-acetoxychlorophyllide a 68 aerobic phototoxicity 38 acetyl carbonyl 204 aerobic phototrophic bacteria 19 Acidiphilium 34, 112, 113, 599, 608 aerobic purple bacteria 19–20 Acidiphilium acidophilum 599 aerobic repression Acidiphilium cryptum 603, 614 CrtJ 716–721 Acidiphilium cryptum JF-5 790, 791, 792 aerobic repressor 784, 785 Acidiphilium rubrum 112, 113 aerobic respiration 149 Acidisphaera 34 aerotaxis 651 Acidithiobacillus 459, 608 AerR 785, 791 Acidithiobacillus ferrooxidans 459, 666 aerR 785, 786, 789 acidophilic purple bacteria 11 affi nity chromatography 849 acid pocket 715 AFFM. See atomic force fl uorescence microscopy (AFFM) acpP 122 AFM. See atomic force microscopy (AFM) acpS 122 AFM topographs 164 ACP synthase 122 Agrobacteria 694 acrylic acid 546 Agrobacterium 702 AcsF 42, 72 Agrobacterium tumefaciens 805 acsF 44, 47, 51, 72, 794 ALA. See δ-aminolevulinate; See 5-aminolevulinic acid (ALA) actin fi lament 486 ALAD. See δ-aminolevulinic acid dehydratase action spectrum 871 ALA dehydratase 60 + – active P QB state 957, 961, 963 ALA synthase 778, 780, 782, 783, 786, 788, 791 acyl carrier protein (ACP) 122 Alcaligenes eutrophus 744 976 Index Alcaligenes faecalis 635 hexagonally packed 945 alcohols 40 LH2 size heterogeneity 948 Alexandrium 48 packing density 946 algae 103 ring size 151 algal blooms 48 antenna absorption transition 203–205 Alkalilimnicola 600 antenna complex 146–151; See also light-harvesting 1 Alkalilimnicola ehrlichei 604, 615 complex; See also light-harvesting 2 complex alkaliphilic purple bacteria 10–11 artifi cial 861 Alkalispirillum 600 synthesis 147 Allochromation vinosum 612, 745 antenna connectivity 170 Allochromatium 8 antenna domain formation 944 Allochromatium minutissimum 607 antenna domains 257, 945, 946, 949 Allochromatium vinosum 3, 4, 6, 103, 384, 515, 596, 601, 604, antenna heterogeneity 944 606, 609, 610, 613, 615, 853 antenna proteins 200–201 Allochromatium warmingii 601 anthraquinone 304, 382, 391 allosteric 791 antibiotic resistance markers 842 alphaproteobacteria 5, 18–19, 59, 98, 99, 111, 112, 581, 597 antimycin 519 phototrophic 597 antimycin A 435, 455, 526 alternative nitrogenase 769 antioxidative 41 amidase 90 anti sigma factor FlgM 645 amino acid APAT 611 distribution 918, 920 APB. See aerobic phototrophic bacteria model sequence 920 apoCyt c 409 motifs 918, 920 apoCyt c heme binding 413 sequence contexts 922 apocytochrome c 407 amino acid sequence 921 apoptosis 527 model 916 AppA 652, 718, 719, 732, 785, 818, 831 5-aminolevulinic acid (ALA) 778, 780, 782, 783, 786, 788, light-responding antirepressor 718 791 regulatory role 718 aminopropanol 82 appA 785 aminopropyltriethoxysilane 862 apparent equilibrium constant 520, 524 ammonium transporter 769–770 apr 603 AmtB 769–770 APS kinase 613, 615 amphiphile 146 APS reductase 615 amphiphilic protein maquettes 905–907 APS reductase pathway 610 AmtB 769–770 Aquifex aeolicus 749 ammonium transporter 769–770 Arabidopsis thaliana 72, 612, 847 anaerobic ammonia oxidation 624 ArcB/ArcA 753 anaerobic aromatic compound ArcB sensor kinase 754 degradation 589–590 Archaea 609, 746 anaerobic benzoate degradation 580–589 Arhodomonas aquaeolei 600 anaerobic benzoate photometabolism 580 aromatic compounds 577–591 anaerobic conditions 72, 523 degradation 577–591 anaerobic respiration 149 aromatic residues 916, 918, 920, 922, 924 anaerobiosis 848 arrA 549 analogs 184 arrB 549 anaplerotic CO2 fi xation 40 ars determinants 662 anaplerotic CO2 incorporation 48 arsABC 673, 675 AnfA 769 arsC gene family 676 anfA 765 arsenate 549, 663 anfHDGK 769 arsenate reductase 676 anfHDK 761 arsenate respiration 549 anhydrorhodovibrin 929, 931 arsenic 548–550 anisotropy decay 243 arsenite 550 annihilation experiments 148 arsenite oxidase 459, 549, 552 Antarctica 4 arsenite oxidation 549, 664 antenna ars operon 663 clustering 945 Arsukibacterium ikkense 601 complex assembly 946 artifi cial antenna complex 861 domain formation 944 artifi cial LH1-type complex 873 heterogeneity 944 Aspergillus nidulans 847 Index 977 assembly 195 B core complexes 172 assembly factor β-barrel 416 LhaA 174 β-carotene 98, 113 assembly factor for LH2 174 β-carotene ketolase 113 assembly pathways 407 β-dodecyl maltoside 260 assembly protein β-galactosidase 780, 789 Surf1 545 β-hydroxydecanoyl-ACP dehydratase 122 assimilatory nitrate reductase (Nas) 548, 637 β-hydroxyl-ACP dehydratase 122 assimilatory sulfate reduction 610, 612–615, 613, 616 β-ketoacyl-ACP reductase 122 asymmetrical ζ-carotene 104 β-ketoacyl-ACP synthase I 122 AT-rich codons 850 β-ketoacyl-ACP synthase II 122 ATB binding β-ketoacyl-ACP synthase III 122 Walker A and B motifs 411 β-octyl-glucoside 185 ATCC17023 critical micelle concentration 185 wild-type strain 849 micelle 185 ATCC17025 780, 782, 791 β-octylglucoside (β-OG) 140, 146, 864 ATCC17029 780, 782 β-oxidation 580, 581, 584, 585, 586, 587 atomic force fl uorescence microscopy (AFFM) 270 β helix 511 atomic force microscopy (AFM) 137, 146, 150, 163, 165, 201, β mutant 338 254, 255, 257, 258, 262, 270, 286, 478, 513, 520, 528, β mutation 347 861, 862, 864–865, 941–951 β polypeptide 175, 188, 205 fast scanning 950 ‘b’ position 454, 456 scan range 950 B-branch 301, 306 tip as nano-dissector 950 electron transfer 348, 958 atomic level structural model B-branch electron transfer 348, 958 photosynthetic unit 287 B-side electron transfer 346–348 atomic models 950 b-type heme 452, 752 atovaquone analog 445 B1020 150 ATP 90, 613 B780 934 ATP-binding cassette (ABC) 410 B798-832 35, 46 ATP-binding cassette transporter complex 410 B800 142, 150, 203, 214, 225–226, 878, 882–885 ATP-synthase 475–493, 942 B800-814 46 ATP:sulfate adenylyltransferase 610 B800-820 46, 150 ATP analog 806 B800-830 148, 150 ATPase 419, 748 B800-850 46, 150 CPx-type 661 B800-B850 920 P-type 661 fl uorescence up-conversion 225 ATPase domain 69 B800 molecule 203 ATP binding site 69 B806 46 ATP dependent oligomers 70 B820 182, 188, 932, 934 ATP hydrolysis 66, 70 dimeric structure 186 ATP production 425 hydrophobic surface area 183 ATP regenerating system 67 NMR experiments 186 ATP regeneration system 74 oligomerization 187 ATP sulfurylase 610, 611, 613, 615, 616 reversible dissociation 183 ATP synthase 254, 262, 264, 279, 476–488, 510, 538 B820-type complex 188 proton translocation 476–488 minimal requirements 190 ATP synthesis 510 B820 complex 157, 175, 183 ATP synthesis/hydrolysis 478–486 chemically synthesized polypeptides 189 auto-induce 844 heterodimeric B820 189 auto-oxidization 438 homodimeric B820 189 autophosphorylation 800, 802, 806 membrane-spanning middle segment 189 RegB 713 N-terminus 189 Avena sativa 815 protein interactions 189 average excitation lifetime 280 proteolysis 189 avoided level crossings 283 shorter synthetic polypeptides 189 Azoarcus 581, 588 B850 142, 214, 878, 885–889 Azotobacter vinelandii 637 B850 ring azoxystobin 442 elliptical deformation 207 B870 934 978 Index B875 150, 927 Mg coordination 184–188 B880 926, 932, 935 binding energy 185 B880 formation 931 modifi ed pigments 915 B890 150 molecule 204, 205 Bacillus 457, 669 distorted conformation 205 Bacillus PS3 479 monomer 338, 341 Bacillus selenitireducens 549, 664 π-π interactions 190 Bacillus subtilis 413, 813, 852 Qy-band 897 back-reaction 148 replacement 305 bacterial artifi cial chromosome (BAC) 45 spectra 897 bacterial plasma membrane 264 stereochemical aspects 915 bacteriochlorin 58, 897 surface area 897 bacteriochlorin exclusion 301 tetrapyrrole ring 42 bacteriochlorin replacement 302 transition dipoles 168 bacteriochlorin ring 141 water ligand 344 (bacterio)chlorophyll 916 bacteriochlorophyll-B850/protein interface 922 (bacterio)chlorophyll binding pocket 916 bacteriochlorophyll-binding proteins statistical analysis 916 synthetic 895, 896–907 binding 916 bacteriochlorophyll/protein interface 915, 916, 922 binding-motifs 916 packing interactions 923 binding pockets 919 bacteriochlorophyll/transmembrane helix interface 923 binding
Recommended publications
  • Int J Syst Evol Microbiol 67 1
    Author version : International Journal of Systematic and Evolutionary Microbiology, vol.67(6); 2017; 1949-1956 Imhoffiella gen. nov.. a marine phototrophic member of family Chromatiaceae including the description of Imhoffiella purpurea sp. nov. and the reclassification of Thiorhodococcus bheemlicus Anil Kumar et al. 2007 as Imhoffiella bheemlica comb. nov. Nupur1, Mohit Kumar Saini1, Pradeep Kumar Singh1, Suresh Korpole1, Naga Radha Srinivas Tanuku2, Shinichi Takaichi3 and Anil Kumar Pinnaka1* 1Microbial Type Culture Collection and Gene Bank, CSIR-Institute of Microbial Technology, Sector 39A, Chandigarh – 160 036, INDIA 2CSIR-National Institute of Oceanography, Regional Centre, 176, Lawsons Bay Colony, Visakhapatnam-530017, INDIA 3Nippon Medical School, Department of Biology, Kyonan-cho, Musashino 180-0023, Japan Address for correspondence* Dr. P. Anil Kumar Microbial Type Culture Collection and Gene Bank, Institute of Microbial Technology (CSIR), Sector 39A, Chandigarh – 160 036, INDIA Email: [email protected] Telephone: 00-91-172-6665170 Running title Imhoffiella purpurea sp. nov. Subject category New taxa (Gammaproteobacteria) The GenBank/EMBL/DDBJ accession number for the 16S rRNA gene sequence of strain AK35T is HF562219. A coccoid-shaped phototrophic purple sulfur bacterium was isolated from a coastal surface water sample collected from Visakhapatnam, India. Strain AK35T was Gram-negative, motile, purple colored, containing bacteriochlorophyll a and the carotenoid rhodopinal as major photosynthetic pigments. Strain AK35T was able to grow photoheterotrophically and could utilize a number of organic substrates. It was unable to grow photoautotrophically. Strain AK35T was able to utilize sulfide and thiosulfate as electron donors. The main fatty acids present were identified as C16:0, C18:1 T 7c and C16:1 7c and/or iso-C15:0 2OH (Summed feature 3) were identified.
    [Show full text]
  • Coupled Reductive and Oxidative Sulfur Cycling in the Phototrophic Plate of a Meromictic Lake T
    Geobiology (2014), 12, 451–468 DOI: 10.1111/gbi.12092 Coupled reductive and oxidative sulfur cycling in the phototrophic plate of a meromictic lake T. L. HAMILTON,1 R. J. BOVEE,2 V. THIEL,3 S. R. SATTIN,2 W. MOHR,2 I. SCHAPERDOTH,1 K. VOGL,3 W. P. GILHOOLY III,4 T. W. LYONS,5 L. P. TOMSHO,3 S. C. SCHUSTER,3,6 J. OVERMANN,7 D. A. BRYANT,3,6,8 A. PEARSON2 AND J. L. MACALADY1 1Department of Geosciences, Penn State Astrobiology Research Center (PSARC), The Pennsylvania State University, University Park, PA, USA 2Department of Earth and Planetary Sciences, Harvard University, Cambridge, MA, USA 3Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA, USA 4Department of Earth Sciences, Indiana University-Purdue University Indianapolis, Indianapolis, IN, USA 5Department of Earth Sciences, University of California, Riverside, CA, USA 6Singapore Center for Environmental Life Sciences Engineering, Nanyang Technological University, Nanyang, Singapore 7Leibniz-Institut DSMZ-Deutsche Sammlung von Mikroorganismen und Zellkulturen, Braunschweig, Germany 8Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT, USA ABSTRACT Mahoney Lake represents an extreme meromictic model system and is a valuable site for examining the organisms and processes that sustain photic zone euxinia (PZE). A single population of purple sulfur bacte- ria (PSB) living in a dense phototrophic plate in the chemocline is responsible for most of the primary pro- duction in Mahoney Lake. Here, we present metagenomic data from this phototrophic plate – including the genome of the major PSB, as obtained from both a highly enriched culture and from the metagenomic data – as well as evidence for multiple other taxa that contribute to the oxidative sulfur cycle and to sulfate reduction.
    [Show full text]
  • Regional Variation of CH4 and N2 Production Processes in the Deep Aquifers of an Accretionary Prism
    Microbes Environ. Vol. 31, No. 3, 329-338, 2016 https://www.jstage.jst.go.jp/browse/jsme2 doi:10.1264/jsme2.ME16091 Regional Variation of CH4 and N2 Production Processes in the Deep Aquifers of an Accretionary Prism MAKOTO MATSUSHITA1, SHUGO ISHIKAWA2, KAZUSHIGE NAGAI2, YUICHIRO HIRATA2, KUNIO OZAWA3, SATOSHI MITSUNOBU4, and HIROYUKI KIMURA1,2,3,5* 1Department of Environment and Energy Systems, Graduate School of Science and Technology, Shizuoka University, Oya, Suruga-ku, Shizuoka 422–8529, Japan; 2Department of Geosciences, Faculties of Science, Shizuoka University, Oya, Suruga-ku, Shizuoka 422–8529, Japan; 3Center for Integrated Research and Education of Natural Hazards, Shizuoka University, Oya, Suruga-ku, Shizuoka 422–8529, Japan; 4Department of Environmental Conservation, Graduate School of Agriculture, Ehime University, Tarumi, Matsuyama 790–8566, Japan; and 5Research Institute of Green Science and Technology, Shizuoka University, Oya, Suruga-ku, Shizuoka 422–8529, Japan (Received May 14, 2016—Accepted July 8, 2016—Published online September 3, 2016) Accretionary prisms are mainly composed of ancient marine sediment scraped from the subducting oceanic plate at a con- vergent plate boundary. Large amounts of anaerobic groundwater and natural gas, mainly methane (CH4) and nitrogen gas (N2), are present in the deep aquifers associated with an accretionary prism; however, the origins of these gases are poorly under- stood. We herein revealed regional variations in CH4 and N2 production processes in deep aquifers in the accretionary prism in Southwest Japan, known as the Shimanto Belt. Stable carbon isotopic and microbiological analyses suggested that CH4 is produced through the non-biological thermal decomposition of organic matter in the deep aquifers in the coastal area near the convergent plate boundary, whereas a syntrophic consortium of hydrogen (H2)-producing fermentative bacteria and H2-utilizing methanogens contributes to the significant production of CH4 observed in deep aquifers in midland and mountainous areas associated with the accretionary prism.
    [Show full text]
  • This Article Was Published in an Elsevier Journal. the Attached Copy
    This article was published in an Elsevier journal. The attached copy is furnished to the author for non-commercial research and education use, including for instruction at the author’s institution, sharing with colleagues and providing to institution administration. Other uses, including reproduction and distribution, or selling or licensing copies, or posting to personal, institutional or third party websites are prohibited. In most cases authors are permitted to post their version of the article (e.g. in Word or Tex form) to their personal website or institutional repository. Authors requiring further information regarding Elsevier’s archiving and manuscript policies are encouraged to visit: http://www.elsevier.com/copyright Author's personal copy Available online at www.sciencedirect.com Geochimica et Cosmochimica Acta 72 (2008) 1396–1414 www.elsevier.com/locate/gca Okenane, a biomarker for purple sulfur bacteria (Chromatiaceae), and other new carotenoid derivatives from the 1640 Ma Barney Creek Formation Jochen J. Brocks a,*, Philippe Schaeffer b a Research School of Earth Sciences and Centre for Macroevolution and Macroecology, The Australian National University, Canberra, ACT 0200, Australia b Laboratoire de Ge´ochimie Bio-organique, CNRS UMR 7177, Ecole Europe´enne de Chimie, Polyme`res et Mate´riaux, 25 rue Becquerel, 67200 Strasbourg, France Received 20 June 2007; accepted in revised form 12 December 2007; available online 23 December 2007 Abstract Carbonates of the 1640 million years (Ma) old Barney Creek Formation (BCF), McArthur Basin, Australia, contain more than 22 different C40 carotenoid derivatives including lycopane, c-carotane, b-carotane, chlorobactane, isorenieratane, b-iso- renieratane, renieratane, b-renierapurpurane, renierapurpurane and the monoaromatic carotenoid okenane.
    [Show full text]
  • SCHELVIS CV Profile 2010
    Curriculum vitae: Johannes Schelvis 09/7/2010 PERSONAL INFORMATION Johannes P. M. Schelvis, Associate Professor Montclair State University Department of Chemistry and Biochemistry 1 Normal Avenue Montclair, NJ 07043 EDUCATION B.S., Physics, 1985, Free University, Amsterdam, Netherlands Ph.D., Biophysics, 1995, University of Leiden, Leiden, Netherlands PROFESSIONAL EXPERIENCE Associate Professor Montclair State University September 2007 – present Assistant Professor New York University September 2000 – August 2007 Postdoctoral Researcher Michigan State University March 1995 - August 2000 HONORS AND AWARDS • Institute Fellow, Margaret and Herman Sokol Institute for the Pharmaceutical Life Sciences at Montclair State University, September 2008 - present • Goddard Fellowship, New York University, 2004 • Whitehead Fellowship for Junior Faculty in Biomedical or Biological Sciences, New York University, 2003. GRANTS AWARDED ACTIVE • "Molecular Mechanisms of Photolyase and Cryptochrome" National Science Foundation, MCB-0920013, August 2009 – July 2012 , $419,453 t.c. (PI) • "Binding of ICER to Its Own Promoter as a Mode of Cooperative Regulation" Margaret and Herman Sokol Institute for Pharmaceutical Life Sciences, September 2008 – August 2011 (1-year no cost extension), $100,000 (PI with Dr. Carlos Molina) • "Light-Driven Damage and Repair of DNA", Faculty Scholarship Program, Montclair State University, 2008 – 2012 , 6 TCH (PI) COMPLETED • "Fingerprinting DNA Damage" Margaret and Herman Sokol Faculty/Student Research Grant Program, July 2008
    [Show full text]
  • Characterisation, Classification and Conformational Variability Of
    Characterisation, Classification and Conformational Variability of Organic Enzyme Cofactors Julia D. Fischer European Bioinformatics Institute Clare Hall College University of Cambridge A thesis submitted for the degree of Doctor of Philosophy 11 April 2011 This dissertation is the result of my own work and includes nothing which is the outcome of work done in collaboration except where specifically indicated in the text. This dissertation does not exceed the word limit of 60,000 words. Acknowledgements I would like to thank all the members of the Thornton research group for their constant interest in my work, their continuous willingness to answer my academic questions, and for their company during my time at the EBI. This includes Saumya Kumar, Sergio Martinez Cuesta, Matthias Ziehm, Dr. Daniela Wieser, Dr. Xun Li, Dr. Irene Pa- patheodorou, Dr. Pedro Ballester, Dr. Abdullah Kahraman, Dr. Rafael Najmanovich, Dr. Tjaart de Beer, Dr. Syed Asad Rahman, Dr. Nicholas Furnham, Dr. Roman Laskowski and Dr. Gemma Holli- day. Special thanks to Asad for allowing me to use early development versions of his SMSD software and for help and advice with the KEGG API installation, to Roman for knowing where to find all kinds of data, to Dani for help with R scripts, to Nick for letting me use his E.C. tree program, to Tjaart for python advice and especially to Gemma for her constant advice and feedback on my work in all aspects, in particular the chemistry side. Most importantly, I would like to thank Prof. Janet Thornton for giving me the chance to work on this project, for all the time she spent in meetings with me and reading my work, for sharing her seemingly limitless knowledge and enthusiasm about the fascinating world of enzymes, and for being such an experienced and motivational advisor.
    [Show full text]
  • Cheminformatics for Genome-Scale Metabolic Reconstructions
    CHEMINFORMATICS FOR GENOME-SCALE METABOLIC RECONSTRUCTIONS John W. May European Molecular Biology Laboratory European Bioinformatics Institute University of Cambridge Homerton College A thesis submitted for the degree of Doctor of Philosophy June 2014 Declaration This thesis is the result of my own work and includes nothing which is the outcome of work done in collaboration except where specifically indicated in the text. This dissertation is not substantially the same as any I have submitted for a degree, diploma or other qualification at any other university, and no part has already been, or is currently being submitted for any degree, diploma or other qualification. This dissertation does not exceed the specified length limit of 60,000 words as defined by the Biology Degree Committee. This dissertation has been typeset using LATEX in 11 pt Palatino, one and half spaced, according to the specifications defined by the Board of Graduate Studies and the Biology Degree Committee. June 2014 John W. May to Róisín Acknowledgements This work was carried out in the Cheminformatics and Metabolism Group at the European Bioinformatics Institute (EMBL-EBI). The project was fund- ed by Unilever, the Biotechnology and Biological Sciences Research Coun- cil [BB/I532153/1], and the European Molecular Biology Laboratory. I would like to thank my supervisor, Christoph Steinbeck for his guidance and providing intellectual freedom. I am also thankful to each member of my thesis advisory committee: Gordon James, Julio Saez-Rodriguez, Kiran Patil, and Gos Micklem who gave their time, advice, and guidance. I am thankful to all members of the Cheminformatics and Metabolism Group.
    [Show full text]
  • (12) United States Patent (10) Patent No.: US 8,501,463 B2 Cox Et Al
    USOO85O1463B2 (12) United States Patent (10) Patent No.: US 8,501,463 B2 Cox et al. (45) Date of Patent: Aug. 6, 2013 (54) ANAEROBC PRODUCTION OF HYDROGEN (56) References Cited AND OTHER CHEMICAL PRODUCTS U.S. PATENT DOCUMENTS (75) Inventors: Marion E. Cox, Morgan Hill, CA (US); 5,350,685 A 9/1994 Taguchi et al. Laura M. Nondorf, Morgan Hill, CA 5,464,539 A 11/1995 Ueno et al. 6,090,266 A 7/2000 Roychowdhury (US); Steven M. Cox, Morgan Hill, CA 6,251,643 B1 6/2001 Hansen et al. (US) 6,299,774 B1 * 10/2001 Ainsworth et al. ........... 210,603 6,342,378 B1 1/2002 Zhang et al. (73) Assignee: Anaerobe Systems, Morgan Hill, CA 6,569,332 B2 * 5/2003 Ainsworth et al. ........... 210,603 2004/0050778 A1 3/2004 Noike et al. (US) 2004/O115782 A1 6/2004 Paterek (*) Notice: Subject to any disclaimer, the term of this FOREIGN PATENT DOCUMENTS patent is extended or adjusted under 35 WO WO-2006-119052 A2 11/2006 U.S.C. 154(b) by 1347 days. OTHER PUBLICATIONS (21) Appl. No.: 11/912,881 Liu et al., 2004. Effects of Culture and Medium Conditions on Hydro gen Production from Starch Using Anaerobic Bacteria. Journal of (22) PCT Fled: Apr. 27, 2006 Bioscience and Bioengineering, vol. 98, No. 4, pp. 251-256.* Zhang et al., Distributed Computer Control of Penicillin Fermenta (86) PCT NO.: PCT/US2OO6/O16332 tion Industrial Production. Proceedings of the IEEE International Conference on Industrial Technology, 1996, pp. 52-56.* S371 (c)(1), New Brunswick, an eppenforf Company, pp.
    [Show full text]
  • Significance of Heme and Heme Degradation in the Pathogenesis Of
    International Journal of Molecular Sciences Review Significance of Heme and Heme Degradation in the Pathogenesis of Acute Lung and Inflammatory Disorders Stefan W. Ryter Proterris, Inc., Boston, MA 02118, USA; [email protected] Abstract: The heme molecule serves as an essential prosthetic group for oxygen transport and storage proteins, as well for cellular metabolic enzyme activities, including those involved in mitochondrial respiration, xenobiotic metabolism, and antioxidant responses. Dysfunction in both heme synthesis and degradation pathways can promote human disease. Heme is a pro-oxidant via iron catalysis that can induce cytotoxicity and injury to the vascular endothelium. Additionally, heme can modulate inflammatory and immune system functions. Thus, the synthesis, utilization and turnover of heme are by necessity tightly regulated. The microsomal heme oxygenase (HO) system degrades heme to carbon monoxide (CO), iron, and biliverdin-IXα, that latter which is converted to bilirubin-IXα by biliverdin reductase. Heme degradation by heme oxygenase-1 (HO-1) is linked to cytoprotection via heme removal, as well as by activity-dependent end-product generation (i.e., bile pigments and CO), and other potential mechanisms. Therapeutic strategies targeting the heme/HO-1 pathway, including therapeutic modulation of heme levels, elevation (or inhibition) of HO-1 protein and activity, and application of CO donor compounds or gas show potential in inflammatory conditions including sepsis and pulmonary diseases. Keywords: acute lung injury; carbon monoxide; heme; heme oxygenase; inflammation; lung dis- ease; sepsis Citation: Ryter, S.W. Significance of Heme and Heme Degradation in the Pathogenesis of Acute Lung and Inflammatory Disorders. Int. J. Mol. 1. Introduction Sci.
    [Show full text]
  • Evolution of the Heme Biosynthetic Pathway in Eukaryotic Phototrophs
    School of Doctoral Studies in Biological Sciences University of South Bohemia in České Budějovice Faculty of Science Evolution of the Heme Biosynthetic Pathway in Eukaryotic Phototrophs Ph.D. Thesis Mgr. Jaromír Cihlář Supervisor: Prof. Ing. Miroslav Oborník, Ph.D. Biology Centre CAS v.v.i., Institute of Parasitology České Budějovice 2018 This thesis should be cited as: Cihlář J., 2018. Evolution of the Heme Biosynthetic Pathway in Eukaryotic Phototrophs. Ph.D. Thesis Series, University of South Bohemia, Faculty of Science, School of Doctoral Studies in Biological Sciences, České Budějovice, Czech Republic. Annotation This thesis is devoted to the evolution of the heme biosynthetic pathway in eukaryotic phototrophs with particular emphasis on algae possessing secondary and tertiary red and green derived plastids. Based on molecular biology and bioinformatics approaches it explores the diversity and similarities in heme biosynthesis among different algae. The core study of this thesis describes the heme biosynthesis in Bigelowiella natans and Guillardia theta, algae containing a remnant endosymbiont nucleus within their plastids, in dinoflagellates containing tertiary endosymbionts derived from diatoms – called dinotoms, and in Lepidodinium chlorophorum, a dinoflagellate containing a secondary green plastid. The thesis further focusses on new insights in the heme biosynthetic pathway and general origin of the genes in chromerids the group of free-living algae closely related to apicomplexan parasites. Declaration [in Czech] Prohlašuji, že svoji disertační práci jsem vypracoval samostatně pouze s použitím pramenů a literatury uvedených v seznamu citované literatury. Prohlašuji, že v souladu s § 47b zákona č. 111/1998 Sb. v platném znění souhlasím se zveřejněním své disertační práce, a to v nezkrácené podobě elektronickou cestou ve veřejně přístupné části databáze STAG provozované Jihočeskou univerzitou v Českých Budějovicích na jejích internetových stránkách, a to se zachováním mého autorského práva k odevzdanému textu této kvalifikační práce.
    [Show full text]
  • (12) Patent Application Publication (10) Pub. No.: US 2016/0186168 A1 Konieczka Et Al
    US 2016O1861 68A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2016/0186168 A1 Konieczka et al. (43) Pub. Date: Jun. 30, 2016 (54) PROCESSES AND HOST CELLS FOR Related U.S. Application Data GENOME, PATHWAY. AND BIOMOLECULAR (60) Provisional application No. 61/938,933, filed on Feb. ENGINEERING 12, 2014, provisional application No. 61/935,265, - - - filed on Feb. 3, 2014, provisional application No. (71) Applicant: ENEVOLV, INC., Cambridge, MA (US) 61/883,131, filed on Sep. 26, 2013, provisional appli (72) Inventors: Jay H. Konieczka, Cambridge, MA cation No. 61/861,805, filed on Aug. 2, 2013. (US); James E. Spoonamore, Publication Classification Cambridge, MA (US); Ilan N. Wapinski, Cambridge, MA (US); (51) Int. Cl. Farren J. Isaacs, Cambridge, MA (US); CI2N 5/10 (2006.01) Gregory B. Foley, Cambridge, MA (US) CI2N 15/70 (2006.01) CI2N 5/8 (2006.01) (21) Appl. No.: 14/909, 184 (52) U.S. Cl. 1-1. CPC ............ CI2N 15/1082 (2013.01); C12N 15/81 (22) PCT Filed: Aug. 4, 2014 (2013.01); C12N 15/70 (2013.01) (86). PCT No.: PCT/US1.4/49649 (57) ABSTRACT S371 (c)(1), The present disclosure provides compositions and methods (2) Date: Feb. 1, 2016 for genomic engineering. Patent Application Publication Jun. 30, 2016 Sheet 1 of 4 US 2016/O186168 A1 Patent Application Publication Jun. 30, 2016 Sheet 2 of 4 US 2016/O186168 A1 &&&&3&&3&&**??*,º**)..,.: ××××××××××××××××××××-************************** Patent Application Publication Jun. 30, 2016 Sheet 3 of 4 US 2016/O186168 A1 No.vaegwzºkgwaewaeg Patent Application Publication Jun. 30, 2016 Sheet 4 of 4 US 2016/O186168 A1 US 2016/01 86168 A1 Jun.
    [Show full text]
  • Comparing the Mechanisms of Metal Action in Bacteria: Insight Into Novel Genes Involved in Silver, Gallium and Copper Resistance and Toxicity in Escherichia Coli
    University of Calgary PRISM: University of Calgary's Digital Repository Graduate Studies The Vault: Electronic Theses and Dissertations 2019-07-25 Comparing the mechanisms of metal action in bacteria: insight into novel genes involved in silver, gallium and copper resistance and toxicity in Escherichia coli Gugala, Natalie Gugala, N. (2019). Comparing the mechanisms of metal action in bacteria: insight into novel genes involved in silver, gallium and copper resistance and toxicity in Escherichia coli (Unpublished doctoral thesis). University of Calgary, Calgary, AB. http://hdl.handle.net/1880/110682 doctoral thesis University of Calgary graduate students retain copyright ownership and moral rights for their thesis. You may use this material in any way that is permitted by the Copyright Act or through licensing that has been assigned to the document. For uses that are not allowable under copyright legislation or licensing, you are required to seek permission. Downloaded from PRISM: https://prism.ucalgary.ca Gene Names GO terms (biological process) Score aaeA aaeA // "yhcQ"carboxylic // "b3241" acid // transport "ECK3230" // "transmembrane transport" -0.0487841 aaeB aaeB // "yhcP"transmembrane // "b3240" // "ECK3229"transport // "carboxylic acid transport" 0.10667059 aaeR aaeR // "yhcS"positive // "qseA" regulation // "b3243" of transcription, // "ECK3232" DNA-templated // "DNA-templated0.18076241 transcription, initiation" // "regulation of transcription, DNA-templated" // "transcription, DNA-templated" aaeX aaeX // "yhcR" // "b3242" //
    [Show full text]