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Posters i01 - o10

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 Vibrio harveyi 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
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
Is charge transfer complex formation essential for
reduction of p-hydroxybenzoate hydroxylase?
Catalytic mechanism of 2-hydroxybiphenyl 3-
Purification and some properties of acetophenone
Mariëlle J. H. Moonen, Ivonne M. C.
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

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
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
Thermus aquaticus.
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
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 b
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
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
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.


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Microsoft word - nease leiden paper 17-10-2008.doc

Paper presented at The First Dutch Balint Conference, Oegstgeest, Netherlands, Oct 17th 2008. Can primary care recover patient-centered medicine? Donald E. Nease, Jr., MD President, American Balint Society Vice President, International Balint Federation Associate Professor of Family Medicine University of Michigan – Ann Arbor, Michigan USA Introduction First, I would like to say a word of thank

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