Poster Abstracts (continued) Blue Light Effects, Photochemistry, Luciferase Class II DNA photolyase from Arabidopsis thaliana contains FAD as cofactor Occurrence of P-flavin binding protein in Vibrio fischerii and properties of the protein Modelling the intermediate IV of the luciferase reaction: characterisation of the complex of 5- decylFMN-4a-OH with Vibrioharveyi luciferase In DNA photolyase from Anacystis nidulans primary electron transfer from tryptophan to FADH+ is followed by oxidation of a tyrosine residue DCRY: A Drosophila photoreceptor protein implicated in light entrainment of circadian rhythm
Matsumoto, Teiichi Tanimura, ShinTogashi, Ryu Ueda and TakeshiTodo
Isolation and characterization of DNA photolyase/cytochrome family in Zebra fish Flavoproteins, 3D Structures Crystal structures of „unactivated” p- hydroxybenzoate hydroxylase
van Berkel, Alex Tepliakov andHerman A. Schreuder
Crystallographic studies of a complex between the ferredoxin-NADP+-reductase from the cyanobacterium Anabaena PCC7119 and its functional partner X-Ray structure of a monomeric subunit of the
A. Gruez, D. Pignol, J. L. Ferrer, M. sulfite reductase from E. coli
Zeghouf, J. Coves, M. Fontecave andJ.-C. Fontecilla-Camps
NMR-studies on FMN-binding protein from Desulfovibrio vulgaris (Miyazaki F) Crystal structures of the tetraheme flavoprotein enzyme fumarate reductase from Shewanella
Terrance E. Meyer, Michael A. Cusanovich, Yves Guisez Jozef J. putrefaciens strain MR1 Crystallographic analysis of C44S NADH oxidase from the human pathogen Streptococcus pyogenes
Derek Parsonage, Al Claiborne andTomitake Tsukihara
A model of the structure of 6-hydroxy-D-nicotine Crystal structure of the flavin reductase Fre from Escherichia coli
Ramaswamy, Vincent Nivière, MarcFontecave and Hans Eklund
Towards the structure of a soluble fumarate reductase
A. Reid, Stephen K. Chapman andMalcolm D. Walkinshaw
Characterization of two E. coli methylenetetrahydrofolate reductase (MTHFR)
Guenther, Martha L. Ludwig andRowena Matthews
mutants, Asp120Asn and Glu28Gln Characterization of glutathione amide reductase from the purple bacterium, Chromatium gracile
Kostanjevecki, Yves Guissez andRobert Bartsch
Domain structure and kinetic analysis of streptococcal L- -glycerophosphate oxidase Refined 2.1 Å structure of the cysteine-sulfenic acid redox center in NADH peroxidase
J. Crane III, Derek Parsonage, Wim G. J. Hol and Al Claiborne
Crystal structure of polyamine oxidase from Zea mays L. at 1.9 Å resolution
Riccardo Angelini, Rodolfo Federico,Paolo Ascenzi and Andrea Mattevi
A new functional model for the Escherichia coli sulfite reductase: the 1 1 complex Monooxygenases Is charge transfer complex formation essential for reduction of p-hydroxybenzoate hydroxylase? Catalytic mechanism of 2-hydroxybiphenyl 3- monooxygenase Purification and some properties of acetophenone
Mariëlle J. H. Moonen, Ivonne M. C. monooxygenase Effect of Substrate and Flavin Activation on the Hydroxylation Reaction of p-Hydroxybenzoate Hydroxylase: Studies of Site Directed Mutants Substituted with 8-Cl-FAD Heterologous Expression and Kinetic Characterization of Human Squalene Monooxygenase Novel two-component phenol hydroxylase from a thermophilic Bacillus strain Development of biocatalyst for acetophenone monooxygenase catalyzed reactions: kinetic and mechanistic characterization of the enzyme and improvement of the biocatalyst Coenzyme recognition by flavoprotein aromatic hydroxylases Flavins and Oxygen, Various Kinetics, mechanism and regulation of elementary steps of catalysis of pyruvate oxidase from Lactobacillus plantarum Studies on the peroxide- reducing system of Thermusaquaticus. Overproduction of Lactococcus lactis NADH oxidase and its application to metabolic engineering
Kleerebezem, Iris I. van Swam andAl Claiborne
Converting a dehydrogenase into an oxidase
Graeme A. Reid, Stephen K. Chapman, Lars Østergaard andMartin L. Goble
What protein features make p-hydroxybenzoate hydroxylase react rapidly with oxygen?
Schreuder, Mariliz Ortiz-Maldonado, DavidBallou and Barrie Entsch
The intermediates involved in the catalytic reaction of cyclohexanone monooxygenase Amine Dehydrogenation Substrate inhibition in trimethylamine dehydrogenase
K. Wilson, Russ Hille and Nigel S. Scrutton
Bacterial amine oxidation through horizontal gene transfer from an eukaryotic source A novel heterotrimeric flavoprotein involved in bacterial nicotine catabolism High level expression and characterization of recombinant human liver MAO B A mechanism for monoamine oxidase involving a redox-active disulfide Involvement of mitochondrial matrix in the holoenzyme formation of dimethylglycine
Ernesto Quagliariello, RoderichBrandsch, Salvatore Passarella and
dehydrogenase Hydrogen tunnelling in amine dehydrogenases from methylotrophic bacteria
Michael J. Sutcliffe and Nigel S. Scrutton
Investigating the mechanism of C-H bond breakage in heterotetrameric sarcosine oxidase from
Michael Sutcliffe and Nigel S. Scrutton
Arthrobacter sp. 1-IN The reductive half-reaction of trimethylamine dehydrogenase with trimethylglutamine Interaction of FAD analogues with the C406A mutant apoenzyme of human liver monoamine oxidase A -Hydroxy Acid Dehydrogenases X-ray studies of recombinant rat kidney long-chain hydroxy acid oxidase and of the recombinant
Barton, Zhi-wei Chen, AhmedBelmouden, K. H. Diêp Lê, Florence
flavin-binding domain of bakers yeast flavocytochrome b2 On the mechanistic value of the dehydrohalogenation reaction of -halogeno hydroxy acids catalysed by FMN-dependent hydroxy acid-oxidising enzymes: a mutational analysis with flavocytochrome b2 D-lactate dehydrogenase model: mechanism of the oxidation of mandelic acids by functionalized flavin mimics with metal ions (S)-mandelate dehydrogenase from Pseudomonas putida: mechanistic roles of the conserved residues H274 and R277 On the role of Asp 180 in L-lactate monooxygenase
Stephen A. Sanders, Ute Müh, CharlesH. Williams Jr. and Vincent Massey
On the mechanism of glucose oxidase
Ben J. L. Williams and Stephen E. J. Rigby
Reaction mechanism of L-lactate oxidase from Aerococcus viridans The substrate specificity of L-mandelate dehydrogenase The membrane-associated (S)-mandelate dehydrogenase from Pseudomonas putida: characterization of a highly active, soluble mutant Acyl-CoA Dehydrogenases Mechanism-based inactivation of medium-chain Acyl-CoA dehydrogenase by a cytotoxic thioester: bioactivation of 5,6-dichloro-4-thia-5-hexenoyl-CoA Synthesis and activity of substrate analogs for glutaryl-CoA dehydrogenase
Donley, Gregory K. Sewall, PatriciaL. Kultgen and Colleen M. Byron
Difference raman studies of hexadienoyl-CoA
Alasdair F. Bell, Jiaquan Wu, Kim M. bound to medium chain acyl CoA dehydrogenase
Sabaj, Avery W. Stephens, Marian T. Stankovich and Peter J. Tonge
Redox potential measurements of short chain acyl- CoA dehydrogenase (SCAD) active site mutants
Becker, James A. Fuchs and MarianT. Stankovich
Interactions of rat acyl-CoA oxidase with substrate analogs used as active-site probes
Kyosuke Sato, Yasuzo Nishina, KiyoshiShiga and Retsu Miura
Biochemical characteristics of recombinant human isovaleryl-CoA dehydrogenase pre-treated with ethylenediaminetetraacetate Probing the mechanism of medium chain acyl-CoA dehydrogenase (MCAD) using spectrally active alternative-substrates and products Substrate chain length specificity of acyl-CoA dehydrogenases: studies on different mutants Probing the active site of the medium chain acyl- CoA dehydrogenase: 4-OH-cinnamoyl-CoA as a sensitive probe of polarization and ionization Substrate polarization of medium chain acyl-CoA dehydrogenase (MCAD)
Peter J. Tonge and Marian T. Stankovich
J Indian Rheumatol Assoc 2002 : 10 : 80 - 96 INDIAN GUIDELINES ON THE MANAGEMENT OF SLE A Kumar Introduction tions. Late mortality i.e. 10 years after diagnosis, on the otherSystemic lupus erythematosus (SLE) is the prototypehand, is mainly attributed to atherosclerotic vascular disease9. of systemic autoimmune diseases. The aetiology is not knownThere is a fair amount of iatrogenic m
Makers of Lipitor Also Made Chemical, Biological Weapons By Dr. Joseph Mercola, M.D. www.mercola.com Long before they began making Lipitor, Pfizer was one ofmany pharmaceutical and chemical companies that developedmilitary weapons, according to a fascinating report writtenmore than four decades ago and now available from TheMemory Hole. The report discusses the company's (then called Ch