Flavins and flavoproteins 1990: proceedings of the Tenth International Symposium, Como, Italy, July 15 - 20, 1990
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| Format: | Tagungsbericht Buch |
|---|---|
| Sprache: | English |
| Veröffentlicht: |
Berlin u.a.
de Gruyter
1991
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| Online-Zugang: | Inhaltsverzeichnis |
| Beschreibung: | XXIII, 945 S. Ill., graph. Darst. |
| ISBN: | 089925666X 3110123738 |
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| 245 | 1 | 0 | |a Flavins and flavoproteins 1990 |b proceedings of the Tenth International Symposium, Como, Italy, July 15 - 20, 1990 |c eds.: B. Curti ... |
| 264 | 1 | |a Berlin u.a. |b de Gruyter |c 1991 | |
| 300 | |a XXIII, 945 S. |b Ill., graph. Darst. | ||
| 336 | |b txt |2 rdacontent | ||
| 337 | |b n |2 rdamedia | ||
| 338 | |b nc |2 rdacarrier | ||
| 650 | 4 | |a Flavins |v Congresses | |
| 650 | 4 | |a Flavoproteins |v Congresses | |
| 650 | 0 | 7 | |a Flavine |0 (DE-588)4154578-3 |2 gnd |9 rswk-swf |
| 650 | 0 | 7 | |a Flavoenzym |0 (DE-588)4154580-1 |2 gnd |9 rswk-swf |
| 655 | 7 | |0 (DE-588)1071861417 |a Konferenzschrift |y 1990 |z Como |2 gnd-content | |
| 689 | 0 | 0 | |a Flavine |0 (DE-588)4154578-3 |D s |
| 689 | 0 | |5 DE-604 | |
| 689 | 1 | 0 | |a Flavoenzym |0 (DE-588)4154580-1 |D s |
| 689 | 1 | |5 DE-604 | |
| 700 | 1 | |a Curti, Bruno |e Sonstige |4 oth | |
| 711 | 2 | |a International Symposium on Flavins and Flavoproteins |n 10 |d 1990 |c Como |j Sonstige |0 (DE-588)5032770-7 |4 oth | |
| 856 | 4 | 2 | |m Digitalisierung TU Muenchen |q application/pdf |u http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=003395487&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |3 Inhaltsverzeichnis |
| 999 | |a oai:aleph.bib-bvb.de:BVB01-003395487 | ||
Datensatz im Suchindex
| _version_ | 1804119638369370112 |
|---|---|
| adam_text | CONTENTS
INTRODUCTORY LECTURE
Flavins and flavoproteins
-
past, present, and future
K. Yagi
3
FLAVIN CHEMISTRY AND PHYSICO-CHEMICAL STUDIES
OF FLAVOPROTEINS
Spectral properties of cyanoalloxazines
J.
Kozioł,
M. M.
Szafran, A. Koziolowa, and
Η.
Szymusiak
19
Phototautomerism of alloxazines in the presence of acetic acid in different media
A. Koziolowa, M. Stroinska, and
M. M.
Szafran
23
Ionisation
properties of reduced, 1,5-dihydroflavin, rates of N(5)-H exchange
with solvent.
S. Ghisla, P. Macheroux,
С
Sanner,
H.
Rüterjans, and F. Müller 27
Photoproduct of
8-hydroxyflavin
K. Matsui, S.
Kasai,
R.
Miura,
and S.
Fujii
33
The breakdown of C(4a)-flavin-peroxides into flavin and a hydroperoxide in
different environments
G.
Merényi,
and J.
Lind 37
Fluorescence spectra of crystalline alloxazine and its methyl derivatives
M. M.
Szafran,
J.
Kozioł,
and P. F. Heelis
41
Comparative fluorescence study of phototautomerism of lumichrome in
dodecylammonium propionate reversed micelles
B. Tyrakowska, A. Koziolowa, P. I. H.
Bastiaens,
and A. J. W.
G. Visser
45
Picosecond fluorescence dynamics of reduced flavins
A. J. W.
G. Visser,
S.
Ghisla, and J. Lee
49
Reaction mechanism of flavin-photosensitized oxidation and reduction of c-type,
cytochromes
M. Roncel, M. Hervas, J.
A. Navarro,
M. A. De la
Rosa, and
G.
Tollin 55
A simple
method for the determination of
redox
potentials
V. Massey
59
Electron spin resonance spectral studies of N-rH flavin coenzyme semiquinones
in flavoenzymes
D. E. Edmondson,
F. Müller, F.
Schaub, and Y. Nisimoto
67
Interflavin
energy transfer as a tool to determine geometrical parameters in
flavoproteins
-η
P. I. H.
Bastiaens,
and A. J. W.
G. Visser
*
BIOSYNTHESIS OF FLAVINS AND FLAVOPROTEINS
Cloning and molecular characterization of the
riboflavin synthase-encoding
gene of Saccharomyces cerevisiae
J. L.
Revuelta,
M.
A. Santos, and
J. J.
Garcia-Ramirez 8
1
FAD synthetase from Brevibacterium ammoniagenes:pio&ess report on cloning
and expression in Escherichia
coli
P. A. Ellison, and
E. F. Pai
»5
Rat brain flavokinase: purification, properties, and comparison to the
enzyme from liver and small intestine
H.
Nakano,
and D. B. McCormick
89
Flavin-dependent expression and modification of
б
-hydroxy-D-nicotine
oxidase
R.
Brandsch
93
Covalent flavinylation of
apo-ó-hydroxy-D-nicotine oxidase
К.
Decker,
H.
Nagursky,
V. Bichler, L.
Mauch, and
R.
Brandsch
101
OXIDASES
The structure of glycolate
oxidase
Y.
Lindqvist
107
Two-photon reactions of dihydroflavin mononucleotide in glycolate
oxidase,
studied by nanosecond laser photolysis
L.
Lindqvist
115
Characterization of glycolate
oxidase
and an active site mutant
P. Macheroux, V. Massey, D. J.
Thiele,
E.
Söderlind,
and
Y.
Lindqvist
119
L-lactate
monooxygenase, proposed active site structure and mechanism
S. Ghisla, and V. Massey
, 123
Lactate oxidase:
mutagenesis and expression of the mycobacterial gene
U.
Müh,
D. A. Giegel,
V. Massey, and
C. H. Williamsjr.
131
Molecular biological studies on structure-function relationship of D-amino
acid
oxidase
Y.
Miyake,
K. Fukui,
К.
Momoi, F. Watanabe, M.
Tada,
M. Miyano, and
S.Takahashi 135
Genomic
organization and
expression
of D-amino acid oxidase
gene
К.
Fukui,
К.
Momoi, F. Watanabe,
M.
Tada,
M. Miyano, and Y. Miyake
143
XI
Expression
of mouse kidney D-amino acid
oxidase
in Escherichia
coli:
purification and characterization of the
recombinant
protein
M.
Tada,
К.
Fukui,
M. Miyano, and Y. Miyaké
147
Purification
of
recombinant mutant porcine D-amino
acid
oxidases
M. Miyano, K. Fukui, F. Watanabe, M.
Tada,
S. Takahashi, and Y. Miyaké
151
Limited proteolysis
studies on the
apo-, holo-, holoenzyme-benzoate
forms
of pig kidney D-amino acid
oxidase
G.
Torri
Tarelli,
M. A. Vanoni,
Α.
Negri, and B.
Curti
155
Reinvestigation
of the role of
lysine
residues in D-amino acid
oxidase
T. Simonie,
L.
Mannucci, A. Negri, G. Tedeschi,
and S.
Ronchi
159
Structural change of a ligand upon complexation with D-amino acid
oxidase
Y.
Nishina,
К.
Sato, and
К.
Shiga
163
D-amino acid
oxidase
expressed under induction conditions is enzymatically
active in microperoxisomes of Rhodotorula gracilis
M. Pilone
Simonetta,
M.
E.
Perotó,
and L.
PoUegioni
167
On the recombination process of apo-D-amino acid
oxidase
from Rhodotorula
gracilis
P. Casalin, L. PoUegioni, B.
Curti,
and M. Pilone
Simonetta
171
FAD analogues as active site probes of Rhodotorula gracilis D-amino acid
oxidase
L.
PoUegioni,
M.
Pilone
Simonetta,
and
S. Ghisla
175
Structural studies on beef kidney D-aspartate
oxidase
A. Negri, G.
Tedeschi,
F. Ceciliani,
T.
Simonie, and S.
Ronchi
179
Modification
of substrate specificity of D-aspartate
oxidase
chemically
modified by phenylglyoxal
G.
Tedeschi, A. Negri,
P.
A. Biondi,
С.
Secchi,
and
S.
Ronchi
189
Kinetic
isotope
effects on flavoprotein
oxidases
P.
F. Fitzpatrick,
C-T. Hsieh,
J. M.
Děnu, and
J. J.
Emanuele
193
Structural and kinetic analysis of
flavine
adenine dinucleotide
modification in alcohol
oxidase
from methylotrophic yeasts
L. V. Bystrykh, R. M. Kellogg, W. Kruizinga, L.
Dijkhuizen, W.
Harder,
J.
Vervoort,
and
W.
J. H.
van Berkei
197
Studies on yeast-derived and mutant glucose
oxidases
S. Chakraborty,
V. Massey, J. Stratton-Thomas, and S. Rosenberg
201
Effect of deglycosylation on the activity and stability of glucose
oxidase
from Aspergillus
niger
H. M.
Kalisz,
R. D.
Schmid,
H. J.
Hecht,
and D. Schomburg
205
-
and l^C-NMR investigations of glucose
oxidase
from
Aspergillus
niger
С.
Sanner,
P. Macheroux,
H.
Rüterjans, F. Müller, and A. Bacher 209
XII
Effect
of hydrogen peroxide on bakers yeast pyridoxaminephosphate
oxidase
under aerobic and anaerobic conditions #
H. Tsuge, K.
Bando,
S. Uchida, K.
Shinohara-Asai, and
Y.
Hatton
-¿ i ¿
MONOOXYGENASES
Chemical functions of
amino
acid residues in the active site of
para-hydroxybenzoate hydroxylase as studied by site directed mutagenesis
and biophysical techniques
B. Entsch, B. A. Palfey, D. P.
Bailou,
and V. Massey
21У
Site-directed mutagenesis of para-hydroxybenzoate hydroxylase from
Pseudomonas
fluorescens
A. H. Westphal, K. Eschrich, W. M. A. M. van
Dongen,
J.
Α. Ε.
Benen,
A.
de Kok, and
W.
J. H.
van Berkei
231
Partial sequences of phenol hydroxylase and similarities with other
flavoenzymes
H. Y.
Neujahr,
and T. Sejlitz
235
l-aminobenzoyl-CoA monooxygenase/reductase, a novel type of
flavoprotein hydroxylase
B. Langkau, S. Ghisla, V. Massey, and G.
Fuchs 239
Structural studies on the porcine liver multisubstrate flavin-containing
monooxygenase
K. K. Korsmeyer, L. L. Poulsen, and D. M. Ziegler
243
The cofactor dependent interaction of molecular oxygen with phenylalanine
hydroxylase
S. W. Bailey, J. P. Crow, and
J. E.
Ayling
247
FLAVIN DEPENDENT BIOLUMNESCENCE
Mechanisms of bacterial luciferase and aromatic hydroxylases
S.-C.
Tu, H.
I. X.
Mager,
R. Shao, K.
W. Cho, and L.
Xi 253
Random and site directed
mutagenesis
of bacterial
luciferase
L. J. Chlumsky, L. H.
Chen,
C. Clark, H. Abu-Soud, M. M. Ziegler,
F. M. Raushel, and T. O.
Baldwin
261
Xenorhabdus luminescens luciferase:
cloning, sequencing, and
overexpression of the encoding genes and substrate inhibition of the
enzyme
L.
Xi,
K. W. Cho, and S.-C.
Tu 265
On the mechanism of bacterial luciferase. 4a,5-dihydroflavins as model
compounds for reaction intermediates
J. W. Eckstein, and S. Ghisla
269
XIII
Kinetic and mechanistic investigation of the bacterial luciferase reaction
F. M. Raushel, H. M. Abu-Soud, L. S. Mullins, W. A. Francisco, and
T. O. Baldwin
273
Electron (charge) transfers in flavin-mediated luminescence
H. I. X.
Mager,
and S.-C.
Tu
277
On the mechanism of dithionite/HoOo-mduced bacterial
bioluminescence
S.-C.
Tu,
and K. W. Cho
281
Structure of FP39Q including its prosthetic group (Q-flavin):
physiological significance of light emitting reaction in luminous bacteria
S.
Kasai,
S.
Fujii,
R. Miura, S.
Odani,
T. Nakaya, and K. Matsui
285
DEHYDROGENASES AND ELECTRON
TRANSFERASES
Crystallographic
studies of medium
chain acyl-CoA dehydrogenase from
pig liver mitochondria
J. J. P. Kim
291
Modulation of flavin reactivity in the acyl-CoA dehydrogenases
С
Thorpe
299
Deuterium solvent isotope effects on the dissociation of the charge
transfer product complex of medium chain acyl-CoA dehydrogenase and FPCoA
L. Niu, J. T. McFarland, and B. A.
Feinberg 307
Aromatic substrate analogues as mechanistic probes for medium-chain
acyl-CoA dehydrogenases
S.
Engst,
and S. Ghisla
311
Inactivation of medium-chain acyl-CoA dehydrogenase from pig kidney by
methylenecyclopropyl-acetyl-CoA: identification of a new type of
flavin-inhibitor adduct
H.-D.
Zeller,
and S. Ghisla
315
Some properties of
Glu-376-Gln
active site mutant of human medium-chain
acyl-CoA dehydrogenase
S.
Engst,
P.
Bross,
J. Stiemke, A.
Schieber,
A. W. Strauss, D. P. Kelly,
I. Rasched, and S. Ghisla
319
On the role of Glu-376 in catalysis of acyl-CoA dehydrogenases
K. Ankele, K.
Melde,
S.
Engst,
P.
Bross,
S. Ghisla, and A. W. Strauss
325
Rat
liver medium-chain acyl CoA
dehydrogenases
directed by complementary
DNAs
differing in their 5 -region
T. Inagaki,
N.
Ohishi, K. Yagi,
N.
Tsukagoshi, S. Udaka, and S. Ghisla
329
XIV
Purification
and some properties of five distinct acyl-CoA dehydrogenases
nom
bovine liver
,.,,
K.
Melde,
and S.Ghisla 33:>
The involvement of a green FAD-containing enzyme in the dehydration of
S-hydroxyvaleryl-CoA to 4-pentenoyl-CoA in Clostridiwn aminovalericum
U.
Eikmanns, and
W.
Buckel 337
Is
glutaryl-CoA dehydrogenase
from Paracoccus denitrificans regulated
by substrate and product binding?
C. M. Byron, M. T. Stankovich, and M.
Húsain ¿41
Two flavo-dehydrogenases catalyzing desaturation of
А
-ring
of
3-ketosteroids:
S-ketosteroid-ÁMehydrogenase
and 3-ketosteroid-
Δ^
-dehydrogenase
from Nocardia
corallina
E.
Itagaki,
T.
Hatta, and
H.
Matsushita
345
The cloning of old yellow enzyme
K.
Saito,
M.
Davio,
О.
Lockridge, and V. Massey
349
Crystallization and characterization of old yellow enzyme
K. M. Fox, S. M. Jacques, and P. A. Karplus
353
Studies on old yellow enzyme reconstituted with the active site probe,
S-fiuoro-S-demethylFMN. Covalent modification and 19F-NMR
R. Miura, S.
Fujii,
К.
Kuroda, and S.
Kasai
357
Two-dimensional NMR studies of Desulfovibrio
vulgáris
and Megasphaera
elsdenii flavodoxin
J.
Vervoort, C.
P.
M.
van Mierlo, and J. LeGall
361
C-NMR studies on cyanylated Megasphaera elsdenii flavodoxin
G. M. Doherty, R. Motherway, S. G. Mayhew, and J. P. G. Malthouse
369
Flavin binding site geometry in Anabaena
7120
flavodoxin. Progress
in determining the flavodoxin solution structure
B. J. Stockman, A. M. Krezel, J. B. Olson, E. S. Mooberry, and
J. L. Markley
377
^CNMR study of NADPH-adrenodoxin
reducíase
reconstituted with
^C-enrichedFAD
S.
Fujii,
Y. Nonaka, M.
Okamoto, and R. Miura
381
Covalent phosphorus groups in flavoproteins: the phosphodiester linkage
in Azotobacter (OP) flavodoxin
D. E. Edmondson, M. Boylan, and M. Taylor
385
Differences in flavin motional dynamics in oxidized and reduced
clostridial flavodoxin as assessed by molecular dynamics simulations
and fluorescence anisotropy
R. Leenders, and A. J. W.
G. Visser
393
XV
A working proposal for the role of the apoprotein in determining the
redox
potential of the flavin in flavoproteins: correlations between
potentials and flavin pKs
L. M.
Schopfer,
M. L.
Ludwig,
and V.
Massey
399
Polarized absorption spectra of flavin mononucleotide in flavodoxin
crystals
L. K. Hanson, G. W.
Christoph,
J.
Hofrichter,
and
M. L.
Ludwig 405
Structural
analysis of fully reduced
Λ.
nidulans flavodoxin
C. L.
Luschinsky,
W.
R.
Dunham,
С.
Osborne,
K. A. Pattridge,
and
M. L.
Ludwig
409
The site-directed mutagenesis of bacterial flavodoxins
R. P. Swenson, G. D. Krey, and M.
Eren
415
Structural characterization of site mutants of clostridial flavodoxin
M. L.
Ludwig,
К.
A. Pattridge,
M.
Eren, and
R. P. Swenson
423
Redox
properties of wild-type and mutant flavodoxins from Desulfovibrio
vulgáris (Hildenborough)
G. P. Curley, M. C. Carr, P. A. O Farrell, S. G. Mayhew, and G. Voordouw
429
Characterization of flavodoxin from the eukariote
Chlorella
fusca
M. L. Peleato, S. Ayora, and C.
Gomez-Moreno
437
Common structural features of a red algal flavodoxin and cyanobacterial
ferredoxins
H. Matsubara, K. Fukuyama, and
L. J.
Rogers
441
Cloning of the ferredoxin-NADP 1 oxidoreductase gene and overexpression of
a synthetic flavodoxin gene from the cyanobacteria Anabaena PCC
7119
M. F. Fillat, W. E.
Borrias,
and P. J.
Weisbeek
445
Structure/function of spinach ferredoxin:NADP+ oxidoreductase
P. A. Karplus
449
Spinach ferredoxin-NADP+reductase: characterization of the enzymes
expressed in Escherichia
coli
A. Aliverti, B.
Curti,
G. Zanetti, S.
Ronchi,
T.
Jansen,
and
R. G.
Herrmann
457
Purification
and characterization of ferredoxin-NADP 1 oxidoreductase
from non-photosynthetic tissues
S. Morigasaki, and K.
Wada
461
Ferredoxin binding site of ferredoxin-NADP+
reducíase
as explored by
limited proteolysis and mutagenesis
G. Gadda,
A. Aliverti, G. Zanetti, and S.
Ronchi
465
Ferredoxins and ferredoxin-NADP+ reductases from Anabaena PCC
7119
and spinach: electrostatic effects on intracomplex electron transfer
M.
С
Walker, J.
A. Navarro,
J. J.
Pueyo,
С.
Gomez-Moreno, and
G.
Tollin 469
XVI
Covalenüy
stabilized electron-transfer complexes:
a redox
active
complex between spinach ferredoxin-NADP4 reductase and Desulfovibrw
vulgáris
flavodoxin
, „
л
w
ι. λί*
G.
Zanetti,
M.
Colombo
Pirola,
F.
Monti,
В.
Curü,
and
S. G. Mayhew
4
о
Structural
analysis of the requirements for the formation of an electron
transfer complex
._„
M. Medina,
С
Blancas,
M. L. Peleato, and C.
Gomez-Moreno
*
*
Intramolecular
electron
transfer
between ferredoxin-NADP4 reductase
and flavodoxin: a laser photolysis study
J. J. Pueyo, M.
С
Walker, G. Tollin, and
С
Gomez-Moreno 48a
Evaluation of secondary structure predictions for enzymes related to
ferredoxin reductase
C. M.
Bruns, and P. A. Karplus
487
Roles of four
cysteine
residues and
lysine
110
in human NADH-cytochrome
be reductase studied by site-directed mutagenesis
K. Shirabe, T. Yubisui, Y. Fujimoto, T. Nagai, T. Nishino, and
M. Takeshita
491
DISULFIDE REDUCTASES
Pyridine nucleotide-disulfide
oxidoreductases-Overview of the family
and some properties of thioredoxin reductase altered by site directed
mutagenesis: C135S and C138S
C. H.
Williams, Jr., A. J. Prongay, B. W.
Lennon,
and J. Kuriyan
497
Structural changes on binding FAD-analogues and on site-directed
mutagenesis of glutathione reductase
G. E.
Schulz,
and U. Ermler
505
Exploration of the coenzyme and
substţate
specificity of glutathione
reductase and its
subunit
assembly
R.
N.
Perham,
N.
S. Scrutton, A. Berry, and M. P. Deonarain
513
Subunit
interactions in the glutathione reductase from Escherichia
coli
A. Berry, M. P. Deonarain,
N.
S. Scrutton, and R.
N.
Perham
521
Active-site mutants of the glutathione reductase from Escherichia
coli
M.
P. Deonarain,
N.
S. Scrutton, A. Berry, and R.
N.
Perham
525
Yeast glutathione reductase: determination of the
redox
potential using
NADH and NAD *
L. D. Arscott, D.
M. Veine,
and
C. H.
Williams, Jr.
529
Glutathione reductase photoreduction by one-electron donors:
stabilization of FAD semiquinone species by complexation
J.
A. Navarro,
M.
Roncel, and G. Tollin
533
XVII
Mouse
glutathione
reducíase cDNA.
Alignment of the deduced
amino
acid sequence with the structural domains of the human enzyme
M. Tutic, D. Werner, and R. H. Schirmer
537
High level expression of human glutathione reductase cDNA in Escherichia
coli
based on multiple mutations in the traslation initiation region
U. S.
Bucheler,
D.
Werner, and
R. H. Schirmer
541
FAD binding properties of brain glutathione reductase
N.
L. Acan, and
E. F.
Tezcan
545
The three-dimensional crystal structure of lipoamide dehydrogenase from
Azotobacter vinelandii at
2.2
Å
resolution
A. Mattevi, A. J. Schierbeek, G. Teplyakova, and W.
G. J. Hol
549
Site-directed mutagenesis studies on lipoamide dehydrogenase from
Azotobacter vinelandii
J. A. E.
Benen,
W.
J. H.
van Berkei, and A.
de Kok 557
Lipoamide
dehydrogenase
from
Azotobacter vinelandii
-
Kinetic studies on wild type and mutant enzymes
J. A.
E. Benen,
N.
A. H. M.
Dieteren,
W.
J. H.
van Berkei, and A.
de Kok 565
Binding studies of the dihydrolipoamide dehydrogenase component (E3)
in the pyruvate dehydrogenase complex
frota
Azotobacter vinelandii
E.
Schulze,
J. A.
E. Benen,
A. H. Westphal, W. J. H. van
Berkei,
and
A.
de Kok 569
Properties of lipoamide dehydrogenase from
E. coli
modified by
site-directed mutagenesis: K53R and I184Y
K. Maeda-Yorita, V. Massey,
C. H.
Williams, Jr.,
N.
Allison,
G. C.
Russell, and J.
R.
Guest
573
Replacement of the active site base in
E. coli
lipoamide dehydrogenase:
spectral and kinetic characterization
C. H. Williams, Jr., L. D. Arscott, D.
Gamm,
N.
Hopkins,
N.
Allison,
and
J. R.
Guest
577
Characterization of the active site mutants (C44S, C49S) of Escherichia
coli
lipoamide dehydrogenase
N.
Hopkins,
C. H.
Williams Jr.,
G. C
Russell, and J. R. Guest
581
FAD-induced dimerization of apo-lipoamide dehydrogenase from Azotobacter
vinelandii and
P
seudomonas
fluorescens
W. J. H.
van Berkei, and
M. C.
Snoek
585
Pig heart lipoamide dehydrogenase: solvent kinetic isotope effects
B.
N.
Leichus, and J.
S. Blanchard
589
Km effects associated with site-directed mutations that reduce the
velocity of one half reaction of a ping-pong mechanism
R. G.
Matthews
593
XVIII
Human
dihydrolipoamide
dehydrogenase: expression and functional
aspects of normal and modified enzymes
M. S.
Patel,
H.
Kim, and
J. E. Jentoft 5
Structure, function and evolution of multiple lipoamide dehydrogenases
of Pseudomonas
putida
J.
A. Palmer,
К.
Hatter, and
J. R. Sokatch
603
Dihydrolipoamide dehydrogenase from Halobacterium volcanii: purification,
characterisation and molecular cloning
N.
Vettakkorumakankav,
K. J.
Stevenson, and
M. J.
Danson
607
Electron-transferring flavoproteins from glycine-metabolizing anaerobic
bacteria
D.
Dietrichs,
M.
Meyer, A. Uhde, W.
Freudenberg,
and J. R. Andreesen
611
The three-dimensional structure of mercuric
ion reducíase
from Bacillus
sp. strain RC607
N.
Schiering, K. Fritz-Wolf, W. Kabsch, M. J. Moore, M. D. Distefano,
С. Т.
Walsh, and E. F.
Pai
615
On the mechanism of mercuric reductase: an alternating site hypothesis
S. M. Miller, V. Massey, D. P.
Bailou,
C. H.
Williams, Jr.,
M. J.
Moore,
and
С. Т.
Walsh
627
The streptococcal NADH peroxidase and NADH
oxidase:
structural and
mechanistic aspects
A. Claiborne, S. A. Ahmed, P. Ross, and H. Miller
639
Sequence fingerprints for the disulfide reductases: application to the
streptococcal NADH peroxidase
S. A. Ahmed, P. Ross, H. Miller, and A. Claiborne
647
The structure of NADH peroxidase from Streptococcus faecalis
T.
Stehle,
G. E.
Schulz,
S. A. Ahmed,
and A. Claiborne
651
Peroxide modification of monoalkylated glutathione reductase: evidence
for stabilization of an active-site cysteine-sulfenic acid intermediate
H. Miller, and A. Claiborne
655
Artificial flavins as probes of the active-site environment and
redox
behavior of the streptococcal NADH peroxidase
S. A. Ahmed, and A. Claiborne
659
Reactivity of the streptococcal NADH
oxidase
reconstituted with
artificial flavins
S. A. Ahmed, and A. Claiborne
663
NADH peroxidase:
pH
profiles and kinetic isotope effects
V. S. Stoll, and J.
S. Blanchard
667
XIX
COMPLEX FLAVOPROTEINS
An active site probe
(6-N3-FAD)
study of milk xanthine
oxidase
T.
Saito,
and
V.
Massey
673
Electron transfer in xanthine oxidase
containing chemically modified
flavins
D.
Shardy, and
R. Hille
677
Studies of electron transfer in xanthine
oxidase
R.
Hille, and R. F. Anderson
681
Evidence for participation of the phosphoseryl residue of xanthine
oxidase
in the
hydroxylaüon
event during enzyme catalysis
S. C. D Ardenne, and D. E. Edmondson
685
ENDOR studies of the molybdenum centre of xanthine
oxidase
B. D.
Howes,
В.
Bennett,
D. J.
Lowe,
and R. C.
Bray
691
Milk xanthine dehydrogenase
J. Hunt, and V. Massey
695
Molecular cloning of cDNA for rat liver xanthine dehydrogenase and its
primary structure
Y. Amaya, K. Yamazaki, M. Sato, K. Noda, T. Nishino, and T. Nishino
699
Cysteine
residues responsible for dehydrogenase-oxidase conversion of
rat liver xanthine dehydrogenase
T. Nishino, Y. Amaya, K. Noda, and T. Nishino
703
Towards an expression system for site-directed mutagenesis studies of
xanthine dehydrogenase
{Drosophila melanogaster
rosy gene)
R.
С
Bray, R. K. Hughes, W. A. Doyle, J. R. S. Whittle,
J. F.
Burke,
and A. Chovnick
707
Fumarate reductase from Escherichia
coli:
molecular approaches to the
understanding of the function of its prosthetic groups
G.
Cecchini,
В. А. С.
Ackrell,
M. K. Johnson, M. T.
Werth, I. Schroder,
D. J.
Westenberg,
and R. P.
Gunsalus
711
Site directed mutagenesis of the putative ligands of the (3FC-4S)
cluster of fumarate reductase of Escherichia
coli
A. Manodori, G.
Cecchini,
M. T.
Werth,
M. K. Johnson,
I.
Schröder,
and
R.
P.
Gunsalus
719
Site-directed mutagenesis of the active site of Escherichia
coli
fumarate reductase
B. А. С
Ackrell, B. Cochran, G.
Cecchini,
I.
Schröder,
and
R. P. Gunsalus
723
XX
Cloning of the flavo-subunit of human succinate dehydrogenase
M. Malcovati, L. Marchetti, T. Zanelli, M. L. Tenchini, L. Benatti,
T.
Simonie,
and M.
Soria
27
The flavoprotein fraction of NADH-ubiquinone reductase from bovine
mitochondria: relationship to a bacterial NAD-reducing hydrogenase
S. J. Pilkington, J. M. Skehel, and J. E. Walker
731
Two related forms of the respiratory chain NADH dehydrogenase
(Complex I) in
Neurospora
mitochondria
T.
Friedrich,
G.
Hofhaus,
G.
Tuschen,
and H.
Weiss
735
Intramolecular electron transfer in trimethylamine dehydrogenase
from bacterium W3A1
R. J.
Rohlfs,
and R. ffille
739
Structure determination of an iron-sulfur flavoprotein
С. С.
Correli,
and
M. L.
Ludwig 743
Glutamate synthase
from Azospirillum brasilense: role of flavins and
iron sulfur centers
M. A. Vanoni, D. E. Edmondson, G. Zanetti, and B.
Curti
749
Kinetic and structural studies on
glutamate
synthase from Azospirillum
brasilense
M. A. Vanoni, L. Nuzzi, M. Rescigno, M. Visentin, P. Accornero,
R. Pelanda, M.
Pilone
Simonetta, G.
Zanetti, and
В.
Curti
755
Sequence motifs in the flavin domain of NADH: nitrate reductase
W.H. Campbell
761
Thermodynamics and electron transfer in nitrate reductase
M. J. Barber, C. J. Kay, and L. P. Solomonson
765
Redox
interconversion
of nitrate reductase activity catalyzed by
photoexcited flavins
M. A. De
la Rosa, M. Roncel, and J.
A. Navarro
769
On some aspects of the catalysis of
lactate
dehydrogenation by
flavocytochrome >2
F. Lederer 773
Substitution of Tyrl43 by Phe in flavocytochrome b2 affects electron
transfer from flavin to acceptors
С
S.
Miles,
S.
К.
Chapman,
G.
A. Reid,
S. A.
White,
F. S. Mathews,
N.
Rouvière,
and F. Lederer
78З
Isolation
and characterization of the flavin domain of flavocytochrome
b2 expressed independently in
E. coli
R. L.
Pallister,
G.
A. Reid,
C. E.
Brunt, C.
S. Miles, and S. K.
Chapman
787
XXI
Direct
measurement of intramolecular electron transfer between the FMN
and
heme
cofactors of yeast flavocytochromes b2 by flash photolysis:
evidence for product-mediated conformation^ gating
M. C
Walker, and G. Tollin
791
Cloning and sequencing of the Hansenula
anomala
flavocytochrome
02
gene
M.
Gervais,
M.
Tegoni, and Y. Risler
797
Hansenula
anomala
flavocytochrome
Ъ<£
loss of electron donor reactivity
of the flavosemiquinone by pyruvate binding
M. Tegoni, F. S. Mathews, and F. Labeyrie
801
Crystal structure of p-cresol methylhydroxylase at
3.0
Å
resolution
F. S. Mathews, Z.-W. Chen, and W. S. Mclntire
805
Interactions in multi-subunit
redox
proteins: NMR study of the cytochrome
subunit
of p-cresolmethylhydroxylase
W. S. Mclntire, F. S. Mathews, S. Bagby, J. A. Charman,
H. A. O.
Hill,
P. C. Driscoll, and
G. L.
McLendon
809
FOLATE
DEPENDENT FLAVOPROTEINS
Stereochemistry of reduction of methylenetetrahydrofolate to
methyltetrahydrofolate catalyzed by mammalian methylene-tetrahydrofolate
reductase
M. A. Vanoni, S. Lee, H. G. Floss, and R. G. Matthews
815
Reconstitution
of apophotolyase with pterin and/or flavin derivatives
M. S.
Jörns,
В.
Wang, S. P. Jordan, and L. P. Chanderkar
819
Chemical modification
of Corynebacterium
sarcosine
oxidase
with
iodoacetamide
H. Suzuki, and Y. Kawamura-Konishi
827
FLAVOPROTEINS
OF
MEDICAL
RELEVANCE
Molecular studies of trypanothione reductase: an antiparasitic
target enzyme
С
Walsh, M. Bradley, S. Sobolov, and F. X. Sullivan
833
Lipoamide dehydrogenase and trypanothione reductase from Trypanosoma
cruzi,
the causative agent of Chagas disease
R. L. Krauth-Siegel, H. Lohrer, K.-D. Hungerer, and T.
Schöllhammer 843
Binding of FAD to BCNU-treated apoglutathione reductase
K. Becker, T.
Schöllhammer,
and R. H. Schirmer
847
XXII
The EGRAC as a measure of the
riboflavin
states in man.
Titration
of
hemoly sate FAD with apoglutathione
reducíase
К.
Becker, and R. H. Schirmer
l
Studies on the role of serine-127 in NADH-cytochrome b5
reducíase
by
site-directed mutagenesis
T.Yubisui,K.Shirabe,andM.Takeshita
»55
Adrenodoxin
reducíase
of mitochondrial cytochrome P450 systems:
structure and regulation of expression
LHanukoglu
859
Squalene epoxidase: the elusive flavoenzyme of
sterol
biosynthesis
D. B. Jordan
865
Expression of membrane-bound flavoenzymes in yeast
P. Urban, X. O. Breakefield, and D. Pompon
869
Binding of MPP* and its analogs to the rotenone/piericidin site of
NADH dehydrogenase (NADH-ubiquinone oxidoreductase)
T. P. Singer, R. R. Ramsay, M. J. Krueger, and S. K. Youngster
873
Membrane-bound and cytosolic 45kDa proteins in human neutrophils and
HL-60 cells
Y. Nisimoto, and H. Otsuka-Murakami
877
Covalently-bound flavin in peroxisomal
L·pipecolic
acid
oxidase
from
primates
S. J. Mihalik, and M.
C. McGuinness
881
Differences in properties of xanthine dehydrogenase and xanthine
oxidase
T. Nishino
885
Biochemical characterization of a mutant human medium-chain acyl-CoA
dehydrogenase present in patients having deficient activity
P.
Bross,
F. Kräuüe,
J. Stiemke, S. Ghisla, I. Rasched, N. Gregersen,
B. S. Andresen,
A. Strauss,
and D. P. Kelly
895
Restriction analysis of the human medium-chain acyl CoA dehydrogenase
(ACADM) genomic region
A. I. F. Blakemore, D. Curtis, P.
С
Engel,
S.
Щутаа,
and
N.
Gregersen
901
NON REDOX-ACTIVE FLAVOPROTEINS
Acetolactate
synthase: a deviant flavoprotein
J. V. Schloss, L. Ciskanik, E. F.
Pai,
and C.
Thorpe
907
XXIII
LIST OF
PARTICIPANTS
915
AUTHOR INDEX
921
SUBJECT INDEX
927
|
| any_adam_object | 1 |
| building | Verbundindex |
| bvnumber | BV005430510 |
| callnumber-first | Q - Science |
| callnumber-label | QP552 |
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| callnumber-subject | QP - Physiology |
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| classification_tum | CHE 832f CHE 670f CHE 667f CHE 673f CHE 820f |
| ctrlnum | (OCoLC)23079730 (DE-599)BVBBV005430510 |
| dewey-full | 574.19/258 |
| dewey-hundreds | 500 - Natural sciences and mathematics |
| dewey-ones | 574 - [Unassigned] |
| dewey-raw | 574.19/258 |
| dewey-search | 574.19/258 |
| dewey-sort | 3574.19 3258 |
| dewey-tens | 570 - Biology |
| discipline | Biologie Chemie |
| format | Conference Proceeding Book |
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| genre | (DE-588)1071861417 Konferenzschrift 1990 Como gnd-content |
| genre_facet | Konferenzschrift 1990 Como |
| id | DE-604.BV005430510 |
| illustrated | Illustrated |
| indexdate | 2024-07-09T16:29:22Z |
| institution | BVB |
| institution_GND | (DE-588)5032770-7 |
| isbn | 089925666X 3110123738 |
| language | English |
| oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-003395487 |
| oclc_num | 23079730 |
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| owner_facet | DE-12 DE-91G DE-BY-TUM DE-M49 DE-BY-TUM DE-355 DE-BY-UBR DE-188 |
| physical | XXIII, 945 S. Ill., graph. Darst. |
| publishDate | 1991 |
| publishDateSearch | 1991 |
| publishDateSort | 1991 |
| publisher | de Gruyter |
| record_format | marc |
| spelling | Flavins and flavoproteins 1990 proceedings of the Tenth International Symposium, Como, Italy, July 15 - 20, 1990 eds.: B. Curti ... Berlin u.a. de Gruyter 1991 XXIII, 945 S. Ill., graph. Darst. txt rdacontent n rdamedia nc rdacarrier Flavins Congresses Flavoproteins Congresses Flavine (DE-588)4154578-3 gnd rswk-swf Flavoenzym (DE-588)4154580-1 gnd rswk-swf (DE-588)1071861417 Konferenzschrift 1990 Como gnd-content Flavine (DE-588)4154578-3 s DE-604 Flavoenzym (DE-588)4154580-1 s Curti, Bruno Sonstige oth International Symposium on Flavins and Flavoproteins 10 1990 Como Sonstige (DE-588)5032770-7 oth Digitalisierung TU Muenchen application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=003395487&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Flavins and flavoproteins 1990 proceedings of the Tenth International Symposium, Como, Italy, July 15 - 20, 1990 Flavins Congresses Flavoproteins Congresses Flavine (DE-588)4154578-3 gnd Flavoenzym (DE-588)4154580-1 gnd |
| subject_GND | (DE-588)4154578-3 (DE-588)4154580-1 (DE-588)1071861417 |
| title | Flavins and flavoproteins 1990 proceedings of the Tenth International Symposium, Como, Italy, July 15 - 20, 1990 |
| title_auth | Flavins and flavoproteins 1990 proceedings of the Tenth International Symposium, Como, Italy, July 15 - 20, 1990 |
| title_exact_search | Flavins and flavoproteins 1990 proceedings of the Tenth International Symposium, Como, Italy, July 15 - 20, 1990 |
| title_full | Flavins and flavoproteins 1990 proceedings of the Tenth International Symposium, Como, Italy, July 15 - 20, 1990 eds.: B. Curti ... |
| title_fullStr | Flavins and flavoproteins 1990 proceedings of the Tenth International Symposium, Como, Italy, July 15 - 20, 1990 eds.: B. Curti ... |
| title_full_unstemmed | Flavins and flavoproteins 1990 proceedings of the Tenth International Symposium, Como, Italy, July 15 - 20, 1990 eds.: B. Curti ... |
| title_short | Flavins and flavoproteins 1990 |
| title_sort | flavins and flavoproteins 1990 proceedings of the tenth international symposium como italy july 15 20 1990 |
| title_sub | proceedings of the Tenth International Symposium, Como, Italy, July 15 - 20, 1990 |
| topic | Flavins Congresses Flavoproteins Congresses Flavine (DE-588)4154578-3 gnd Flavoenzym (DE-588)4154580-1 gnd |
| topic_facet | Flavins Congresses Flavoproteins Congresses Flavine Flavoenzym Konferenzschrift 1990 Como |
| url | http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=003395487&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
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