Flavins and Flavoproteins: Proceedings of the Eighth International Symposium, Brighton, England, July 9–13, 1984

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Flavins and Flavoproteins

Proceedings of the Eighth International Symposium, Brighton, England, July 9–13, 1984

Edited by: , and

Language: English

Published/Copyright: 1984

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Frontmatter
I

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Preface
V
R.C. Bray, P.C. Engel and S.G. Mayhew

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Organising Committee/Local Committee/Acknowledgements
IX

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Contents
XI

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Participants
XXXI

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Flavin Chemistry
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The influence of hydrogen bond formation with the N(l) atom on the orbital structure of flavin
3
Franz Müller, Jan Kees Eweg, Viola Szczesna and Ben Hesper

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Spectral and photochemical properties of alloxazines
17
Jacek Kozioł, Anna Koziołowa, Wojciech Babś, Jan Dawidowski, Danuta Panek-Janc, Małgorzata Stroińska, Violetta Szczęsna, Henryk Szymusiak and Bożena Tyrakowska

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π...π-interactions of flavins : novel coenzyme models of the cyclophane type
21
Matthias F. Zipplies and Heinz A. Staab

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A laser flash photolysis study of the triplet states of lumichromes
25
Paul F. Heelis and G. O. Phillips

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The dark formation of radicals in flavinium cation/acid systems
29
R. Addink and H.I.X. Mager

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ENDOR studies on flavin radicals
33
Michael Bock, Martin Elsner and Harry Kurreck

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On the role of some flavin adducts as one-electron donors
37
H.I.X. Mager and R. Addink

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Photoinactivation of flavin redox catalysis: the reductive flavin photoadduct formation
41
Ulrich Ott, Rainer Traber and Horst E.A. Kramer

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Flavin oxygen chemistry brought to date
45
Thomas C. Bruice

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Pulse radiolysis studies on the equilibria between reduced and oxidized free flavin species and the effect of molecular oxygen
57
Robert F. Anderson

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Effect of pH on the oxidation-reduction properties of 8α - imidazole flavins
61
Gary Williamson and Dale E. Edmondson

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Studies of intermediates in reactions of flavins and sulphydryl compounds
67
P.S. Surdhar and D.A. Armstrong

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A kinetic study on the acid-catalysed phosphate migration in riboflavin phosphates
71
Peter Nielsen, Peter Rauschenbach and Adelbert Bacher

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Chemical structure of nekoflavin
75
Kunio Matsui and Sabu Kasai

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Flavoprotein Structure
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Binding mode and action of FAD in glutathione reductase
81
G.E. Schulz

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Active site chemical modification and sequencing of flavoproteins
95
Charles H. Williams, L. David Arscott and Richard P. Swenson

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Molecular genetic approaches to the study of E. coli flavoproteins
111
J. R. Guest and D. W. Rice

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Glutathione reductase: mutation, cloning and sequence analysis of the gene in E. coli
125
Shaun Greer and Richard N. Perham

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The coenzyme binding site of glutathione reductase. Correlation of X-ray studies with kinetic data
139
Emil F. Pai, Elke Horn and Georg E. Schulz

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¹³C-NMR study on the active sites of lipoamide dehydrogenase and glutathione reductase
143
Willy A.M. van den Berg, Jacques Vervoort, Chrit T.W. Moonen, Franz Müller, Inger Carlberg and Bengt Mannervik

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X-ray crystallographic studies on lipoamide dehydrogenase from Azotobacter vinelandii
147
A.J. Schierbeek, J. Drenth and W.G.J. Hol

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Mobility of lipoamide dehydrogenase in and out of the pyruvate dehydrogenase complex from Azotobacter vinelandii
149
Arie de Kok and Antonie J.W.G. Visser

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Partial amino acid sequence of pig heart lipoamide dehydrogenase
153
L. David Arscott, Martin Berman and Charles H. Williams

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The amino acid sequence encompassing the active site histidine residue of lipoamide dehydrogenase from Escherichia coli labelled with a bifunctional arsenoxide
157
Charles F.B. Holmes and Kenneth J. Stevenson

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Inactivation of pig heart lipoamide dehydrogenase by 1,3-dibromoacetone
161
James S. Lee and Charles H. Williams

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The evolution of mercuric reductase, and a redox transfer model for mercuric ion detoxification in bacteria
165
Nigel L. Brown and Dean Goddette

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Structural studies on ferredoxin-NADP⁺ oxidoreductase from Spirulina, a blue-green alga
169
Keishiro Wada, Yoshio Yao, Toshiaki Tamura, Hiroshi Matsubara and Keiun Kodo

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The amino acid sequence and partial tertiary structure of ferredoxin-NADP⁺ oxidoreductase from spinach
173
P. Andrew Karplus, Jon R. Herriott and Kenneth A. Walsh

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On the nature of ferredoxin: ferredoxin-NADP⁺ reductase complex
175
Masateru Shin and Naoko Sakihama

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Properties of a cross-linked complex between ferredoxin-NADP⁺ reductase and ferredoxin
179
Giuliana Zanetti and Bruno Curti

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On the enigma of old yellow enzyme's spectral properties
183
Jan K. Eweg, Franz Müller, Willem J.H. van Berkel and Ben Hesper

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"On the enigma of old yellow enzyme's spectral properties"
191
V. Massey, L. M. Schopfer and W. R. Dunham

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NMR studies on the old yellow enzyme
211
Wolf-Dieter Beinert, Heinz Rüterjans and Franz Müller

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Structural and kinetic characteristics of dimethylglycine dehydrogenase and sarcosine dehydrogenase
215
Robert J. Cook, David H. Porter, Kunio S. Misono and Conrad Wagner

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Evidence for two spatially distinct domains on each subunit of methylenetetrahydrofolate reductase
217
Rowena G. Matthews, Maria A. Vanoni, Shahrokh Khani, James F. Hainfeld and Joseph Wall

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Structure of NADH-cytochrome b₅ reductase of human erythrocytes
221
Toshitsugu Yubisui, Toshiyuki Miyata, Sadaaki Iwanaga, Minoru Tamura, Satoshi Yoshida and Masazumi Takeshita

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Structural comparison of the succinate dehydrogenase and fumarate reductase of Escherichia coli
225
J. R. Guest, M. G. Darlison, R. J. Wilde and D. Wood

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Lack of assembly of succinate and NADH-ubiquinone oxidoreductases in iron-deficient rat skeletal muscle mitochondria
229
Brian A.C. Ackrell, Bruce Cochran, Kent Larson, Edna B. Kearney, John J. Maguire and Peter R. Dallman

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Crystal structure study of trimethylamine dehydrogenase
233
F. Scott Mathews, Louis W. Lim and N. Shamala

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The flavin domain of assimilatory NADH: nitrate reductase from Chlorella vulgaris
247
Larry P. Solomonson and Michael J. Barber

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Polarized absorption spectra of flavocytochrome b₂ single crystals
251
Andrea Mozzarelli, Mariella Tegoni and Gian Luigi Rossi

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FMN-protein interactions in flavodoxin from A. nidulans
253
Martha L. Ludwig, Katherine A. Pattridge and George Tarr

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Photochemical formation of a stable red derivative of flavodoxin
261
Stephen G. Mayhew and Vincent Massey

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Desulfovibrio vulgaris flavodoxin. A ¹³C and ¹⁵N NMR investigation
269
Jacques Vervoort, Franz Müller, Jean LeGall, Adelbert Bacher and Helmut Sedlmaier

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¹³C-NMR study on the interaction of riboflavin with riboflavin-binding protein
273
Retsu Miura, Hiromasa Tojo, Shigeru Fujii, Toshio Yamano and Yoshihiro Miyake

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The structure of glycolate oxidase from spinach
277
Ylva Lindqvist and Carl-Ivar Brändén

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ENDOR studies of flavoproteins
289
Norbert Bretz and Harry Kurreck

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Resonance Raman study on the complexes of D-amino acid oxidase
291
Yasuzo Nishina, Kiyoshi Shiga, Retsu Miura, Hiromasa Tojo, Yoshihiro Miyake, Toshio Yamano and Hiroshi Watari

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The role of arginines in D-amino acid oxidase
295
Mirella P. Simonetta, Stefania Galliani, Maria A. Vanoni, Severino Ronchi and Bruno Curti

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The effect of the methylation of histidine-217 in pig kidney D-amino acid oxidase on ligand binding and on catalysis
301
Richard P. Swenson, Charles H. Williams and Vincent Massey

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Stoichiometry of the self-association of D-amino acid oxidase
305
Hiromasa Tojo, Kihachiro Horiike, Kiyoshi Shiga, Yasuzo Nishina, Hiroshi Watari and Toshio Yamano

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³¹P NMR and chemical studies on the phosphorus residues in milk xanthine oxidase
309
Dale E. Edmondson, Michael D. Davis and Franz Müller

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Specific modification of NAD⁺ binding site of chicken liver xanthine oxidase with 5' - p - fluoro - sulphonylbenzoyladenosine
319
Tomoko Nishino, Takeshi Nishino and Keizo Tsushima

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Studies by electron paramagnetic resonance spectroscopy of the environment of the metal in the molybdenum cofactor from xanthine oxidase
323
T.R. Hawkes and R.C. Bray

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Coupling between Mo(V) and reduced Fe/S 1 centres in aldehyde oxidase and xanthine oxidase
325
Graham N. George

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Partial amino acid sequence of L - lactate oxidase from M. smegmatis
331
David A. Giegel, Vincent Massey and Charles H. Williams

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Chemical modification of sulphydryl groups in p - hydroxybenzoate hydroxylase from Pseudomonas fluorescens
335
Willem J.H. van Berkel, Franz Müller, Wicher J. Weijer, Peter A. Jekel and Jaap J. Beintema

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Chemical modification of phenol hydroxylase by p-nitrobenzenes ulphonyl fluoride
339
C. Torsten Sejlitz and Halina Y. Neujahr

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Studies of 2,5-diketocamphane monooxygenase from Pseudomonas putida ATCC 17453
343
David G. Taylor and Peter W. Trudgill

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Recent progress in bioluminescence: cloning of the structural genes encoding bacterial luciferase, analysis of the encoded sequences, and crystallization of the enzyme
345
Thomas O. Baldwin, Timothy C. Johnston and Rosemarie Swanson

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Probing the bacterial luciferase aldehyde site by affinity and photoaffinity labeling
359
Shiao-Chun Tu and Aaron Fried

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The catalytic turnover of bacterial luciferase produces a quasi-stable species of altered conformation
371
Nabil K. AbouKhair, Miriam M. Ziegler and Themas O. Baldwin

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Electron microscopy and X-ray diffraction studies on heavy riboflavin synthase from Bacillus subtilis
375
Rudolf Ladenstein, Birgit Meyer, Robert Huber, Harald Labischinski, Klaus Bartels, Hans-Dieter Bartunik, Luis Bachmann, Heide C. Ludwig and Adelbert Bacher

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Heavy riboflavin synthase from Bacillus subtilis. Primary structure and reaggregation of the B subunits
379
Heide C. Ludwig, Friedrich Lottspeich, Agnes Henschen, Rudolf Ladenstein and Adelbert Bacher

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Enzyme Reaction Mechanisms
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Mechanism of α,β-dehydrogenation of fatty acid CoA derivatives by flavin enzymes
385
Sandro Ghisla

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Butyryl-CoA dehydrogenase: Aspects of acceptor and substrate specificity
403
Paul C. Engel, Gary Williamson and Lee Shaw

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Oxygen reactivity of butyryl-CoA dehydrogenase from Megasphaera elsdenii and from ox liver mitochondria
413
Patricia Ellison, Lee Shaw, Gary Williamson and Paul C. Engel

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Suicide inactivation of short-chain acyl-CoA dehydrogenases by propionyl-CoA. Formation of a substrate - flavin adduct
417
Lee Shaw and Paul C. Engel

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Structure of the flavin N-5 adduct free radical obtained following inhibition of short-chain acyl-CoA dehydrogenase by propionyl-CoA
421
Graham N. George, Lee Shaw, Robert C. Bray and Paul C. Engel

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Purification and properties of five distinct acyl-CoA dehydrogenases from rat liver mitochondria
435
Yasuyuki Ikeda, Kazuko O. Ikeda and Kay Tanaka

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Mechanism of action of short-chain, medium-chain and long-chain acyl-CoA dehydrogenases isolated from rat liver
439
Yasuyuki Ikeda, David Hine, Kazuko O. Ikeda and Kay Tanaka

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Inactivation of pig kidney general acyl-CoA dehydrogenase by 2-alkynoyl-CoA derivatives
443
Kurt Freund, John P. Mizzer and Colin Thorpe

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On the inactivation of general acyl-CoA dehydrogenase from pig kidney by methylenecyclopropyl-acetyl-CoA, a metabolite of hypoglycin
447
Hans-Dieter Zeller and Sandro Ghisla

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Structure-function correlation in B-oxidation enzymes
451
Camilo Rojas, William Gustafson, Jack Schmidt, Dan Domanski, Benjamin A. Feinberg and James T. McFarland

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Purification and characterization of glutaryl-CoA dehydrogenase, electron transfer flavoprotein and ETF-CoQ oxidoreductase from Paracoccus denitrificans
455
Mazhar Husain and Daniel J. Steenkamp

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Reactions of ETF and ETF-CoQ oxidoreductase
459
D.J. Steenkamp, R.R. Ramsay and M. Husain

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Correlation between redox state of ETF and dehydrogenation of octanoyl-CoA
463
Carole L. Hall

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Some observations on an acrylyl-CoA reductase from Clostridium kluyveri and an NADH-dependent fumarate reductase from Enterobacter agglomerans
467
Helmut Sedlmaier, Mathias Bühler, Richard Feicht, Johann Bader and Helmut Simon

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Characterization of the mode of electron transport of NADPH-adrenodoxin reductase
471
Toshio Yamano, Yasuki Nonaka and Shigeru Fujii

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Studies on forward and reverse reactions of adrenodoxin reductase by electronic and NMR spectroscopy
485
Y. Nonaka, S. Fujii and T. Yamano

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Transient kinetics of ferredoxin-NADP⁺ reductase reaction
489
Shinya Yoshikawa, Norihiro Ohnishi, Aiko Morigiwa, Katsuhito Takeshima, Midori Matsumoto, Kyoko Nishiyama, Hiroshi Matsubara and Keiun Kodo

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Some new ideas about the possible regulation of redox potentials in flavoprotein, with special reference to flavodoxins
493
Chrit T.W. Moonen, Jacques Vervoort and Franz Müller

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Methylenetetrahydrofolate reductase: an imperfect enzyme?
497
Maria A. Vanoni and Rowena G. Matthews

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Probing the catalytic mechanism of glutathione reductase with 2,4,6-trinitrobenzenesulphonate
501
Inger Carlberg and Bengt Mannervik

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Multifunctionality of yeast glutathione reductase
505
C.S. Tsai, J.R.P. Godin and Y.H. Tsai

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The reaction between NADPH and mercuric reductase
509
Lena Sahlman, Sven Lindskog, Anne-Marie Lambeir and H. Brian Dunford

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Dehydrohalogenation and intermolecular hydrogen transfer reactions catalyzed by some lactate-oxidizing enzymes
513
Florence Lederer

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On the mechanism of inactivation of flavocytochrome b₂ (baker's yeast) by acetylenic substrates
527
Denis Pompon and Florence Lederer

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Intermolecular hydrogen transfer during transhydrogenation catalysed by flavocytochrome b₂ and lactate oxidase
529
Philippe Urban and Florence Lederer

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Product binding as modulator of flavin redox parameters: a mechanism of activity control in dehydrogenase-e^-transferase?
531
Françoise Labeyrie, Jean-Marc Janot and Mariella Tegoni

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T-jump investigation of intramolecular electron exchanges in Hansenula anomala yeast flavocytochrome b₂, L-lactate-cytochrome c oxidoreductase
535
Mariella Tegoni, Françoise Labeyrie, Maria Chiara Silvestrini and Maurizio Brunori

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A pulse radiolysis study of flavocytochrome b₂: differences in reactivity with carboxylate radicals between flavin and haem b₂
539
Chantal Capeillère-Blandin and Christiane Ferradini

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The distribution of reducing equivalents among some species in succinate dehydrogenase upon reduction by succinate
543
Silvia Pagani and Franco Bonomi

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Ionic species of the flavin and the catalytic cycle of succinate dehydrogenase
547
Franco Bonomi and Silvia Pagani

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ESR spectroscopic studies of succinate dehydrogenase and fumarate reductase from Escherichia coli
551
Richard Cammack, Daulat S. Patil, Caro Condon, Peter Owen, Stewart T. Cole and Joel H. Weiner

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Fumarate reductase from Escherichia coli requires the frdC and frdD gene products for quinone reductase activity
555
Gary Cecchini, Brian A. C. Ackrell, Edna B. Kearney and Robert P. Gunsalus

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Glutamate synthase from Azospirillum brasilense
559
Sabina Ratti, Bruno Curti and Giuliana Zanetti

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Oxidation-reduction properties of glycolate oxidase
565
Charles Pace and Marian Stankovich

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Studies with the flavin-dependent alcohol oxidase from yeast: properties and catalytic mechanism
569
Johanna Geissler, Peter M.H. Kroneck and Sandro Ghisla

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Pulse radiolysis studies on the formation and decay of the flavin 4a-hydroperoxide species of glucose oxidase
573
Robert F. Anderson, Vincent Massey and Lawrence M. Schopfer

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E.coli pyruvate oxidase: a hysteretic enzyme
577
Michael W. Mather and Robert B. Gennis

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Mechanism and functionality of FMN in liver pyridoxine (pyridoxamine) 5'-phosphate oxidase
581
Delores M. Bowers-Komro and Donald B. McCormick

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Enzymatic properties of yeast pyridoxamine-P oxidase
585
Haruhito Tsuge, Toshitaka Okada, Izumi Nakane, Shinji Uchida, Reiko Sugiyama and Kazuji Ohashi

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A photo-labelling reagent of brain pyridoxine-5-P oxidase
589
J. E. Churchich

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Non-stereospecific reduction of monoamine oxidase from bovine liver by analogs of amphetamine
595
Walter Weyler, James I. Salach, R.T. Coutts and G.B. Baker

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The kinetics of NADPH-dependent reduction of FAD and cytochrome b in a solubilised preparation of the superoxide generating oxidase of neutrophils
599
Andrew Cross, John Parkinson and Owen Jones

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Flavoprotein monooxygenases
605
David P. Ballou

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The nature of the 4a-hydroperoxyflavin in the mammalian flavin-containing monooxygenase
619
Kenneth Jones and David P. Ballou

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The effect of pH and ionic strength on the binding of NADPH and NADPH analogues to p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens: the importance of monopole-monopole and monopole-dipole interactions
623
Robert A. Wijnands, Johan W. van Leeuwen, Willem J.H. van Berkel and Franz Müller

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Kinetic mechanism of the reductive half of reaction catalysed by sailcylate hydroxylase
627
Lee-Ho Wang and Shiao-Chun Tu

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The pH dependence of enzyme-phenol complexes of phenol hydroxylase
631
Halina Y. Neujahr

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Differential induction and characterization of flavoprotein hydroxylases in Pseudomonas cepacia
635
Riyad Y. Hamzah and Shiao-Chun Tu

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Steroid monoxygenase from Cylindrocarpon radicicola. An FAD-containing Baeyer-Villiger type oxygenase
639
Eiji Itagaki and Masayuki Katagiri

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Unusual properties of the flavocytochrome p-cresol methylhydroxylase
643
William S. McIntire, Steven C. Koerber, Craig W. Bohmont and Thomas P. Singer

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Identification of the luciferase-bound flavin-4a-hydroxide as the primary emitter in the bacterial bioluminescenee reaction
657
Manfred Kurfürst, J. Woodland Hastings, Sandro Ghisla and Peter Macheroux

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Studies on the bacterial luciferase reaction: isotope effects on the light emission. Is a "CIEEL" mechanism involved?
669
Peter Macheroux, Sandro Ghisla, Manfred Kurfürst and J. Woodland Hastings

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Probes for the active site of bacterial luciferase
673
Frank McCapra, Christopher S. J. Walpole and Ian P. Street

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The cellobiose oxidoreductases of Sporotrichum pulverulentum
679
Fraser F. Morpeth

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The equilibration of reducing equivalents within milk xanthine oxidiase
683
Russ Hille

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Reactions between xanthine oxidase and 4-hydroxy-7-azapteridine
687
Richard C. Stewart and Vincent Massey

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“Type 1” and “Type 2” rapid and slow EPR signals from the molybdenum centres of molybdenum-containing hydroxylases and their significance
691
R.C. Bray, G.N. George, S. Gutteridge, F.F. Morpeth and N. Turner

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Re-sulphuration of xanthine oxidase
695
A. Ventom and R.C. Bray

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Reactivation of desulpho-xanthine oxidase by an enzymatic system
699
Takeshi Nishino, Chikako Usami and Keizo Tsushima

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The existence of desulpho-xanthine dehydrogenase in rat liver
703
Tadashi Ikegami, Takeshi Nishino and Keizo Tsushima

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The structures and catalytic mechanisms of molybdenum centres in enzymes studied by e.p.r and X-ray spectroscopy
707
R.C. Bray

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Biochemistry of naturally-occurring deazaflavin coenzymes
723
Christopher Walsh

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Interaction of the herbicide sulfometuron methyl with acetolactate synthase: a slow-binding inhibitor
737
John V. Schloss

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The rate-determining step in pteridine-dependent monooxygenases is not ring cleavage
741
David Pike, Mary Hora, Steven Bailey and June Ayling

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The one-electron reduction of riboflavin-binding protein
745
M. Faraggi and Michael H. Klapper

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Modified Flavins in Flavoproteins
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8-azidoflavins: photoaffinity labels for flavoproteins
751
Sandro Ghisla, Paul F. Fitzpatrick and Vincent Massey

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Glutathione reductase species containing FAD analogues
755
R.L. Krauth-Siegel, R.H. Schirmer and S. Ghisla

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Flavin analogue studies of pig kidney electron transferring flavoprotein
761
Robert J. Gorelick and Colin Thorpe

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Chemically modified flavins as probes of phenol hydroxylase structure and function
765
Kristina Detmer and Vincent Massey

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4-thioflavins as active site probes of flavoproteins: reaction with sulphite and formation of 4-hydroxy-4-sulphonylflavins
769
Al Claiborne, Vincent Massey, Monika Biemann and Sandro Ghisla

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Oxygen reactivity of 4-thio-FAD p-hydroxybenzoate hydroxylase
773
Al Claiborne, Lawrence M. Schopfer and Vincent Massey

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Oxygen reactions of para-hydroxy benzoate hydroxylase containing 6-hydroxy-FAD
777
Barrie Entsch and Vincent Massey

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The effect of pH and modifications in position 8 on the oxidation of reduced p-hydroxybenzoate hydroxylase
781
L.M. Schopfer, Albert Wessiak and Vincent Massey

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Reaction of bacterial luciferase from Vibrio harveyi with 8-substituted flavins
785
Lorenzo Chen and Thomas O. Baldwin

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Biomedical Aspects
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Intestinal absorption of riboflavin
791
Sabu Kasai, Hideko Nakano, Hirokazu Matsukawa, Yoshihiro Miyake and Kunio Matsui

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Transfer of hydrogen atoms from pentose phosphate to the xylene ring of riboflavin
795
P.J. Keller, H.G. Floss, Q. Le Van, G. Neuberger, P. Nielsen and A. Bacher

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Biosynthesis of riboflavin Enzymatic formation of 6,7-dimethyl-8-ribityllumazine
799
A. Bacher, P. Nielsen, G. Neuberger and H. G. Floss

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Cell-free biosynthesis of lipoamide dehydrogenase
803
Kichiko Koike, Akihiko Tsuji, Yoshishige Urata, Matsuko Moriyasu and Masahiko Koike

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Covalently ¹⁴C-riboflavin-labeled proteins in Arthrobacter oxidans and their possible relationship to 6-hydroxy-D-nicotine oxidase
807
Karl Decker, Henry Reeves and Roderich Brandsch

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Electron immunochemical localization of 6-hydroxy-nicotine oxidases in Arthrobacter oxidans
811
James R. Swafford, Henry C. Reeves, Roderich Brandsch and Karl Decker

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Cloning in Escherichia coli of the 6-hydroxy-D-nicotine oxidase gene from Arthrobacter oxidans
815
Roderich Brandsch

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Hydroxylation of riboflavin 7- and 8-methyl groups in mammals
819
Kunio Yagi, Nobuko Ohishi and Hiroshi Ohkawa

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Mammalian metabolism of flavins
833
D.B. McCormick, W.S.A. Innis, A.H. Merrill and S.-S. Lee

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Flavoenzymes as drug targets
847
R. Heiner Schirmer, Florian Lederbogen, R. Luise Krauth-Siegel, Gerhard Eisenbrand, Georg Schulz and Albrecht Jung

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Studies on Esherichia coli photolyase: role of flavin in DNA repair
861
Marilyn Schuman Jorns, Gwendolyn B. Sancar and Aziz Sancar

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Electron transfer to nitrogenase in K-pneumoniae nifF gene cloned and the gene product, a flavodoxin, purified and partially characterised
875
J. Deistung, S. Hill, R.N.F. Thorneley, F. Cannon and M. Cannon

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Practical Applications of Flavoprotein Studies
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In vitro synthesis of (bio)chemicals using flavin-containing enzymes
879
Colja Laane, Riet Hilhorst, Ruud Spruijt, Koen Dekker and Cees Veeger

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Flavin cofactors covalently attached to electron-conducting supports: electrochemical and enzyme activity
893
Lemuel B. Wingard, Krishna Narasimhan and Osato Miyawaki

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Luminometric determination of immunoadsorbed flavoproteins and of flavin adenine dinucleotide
897
Ari Hinkkanen and Karl Decker

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Flavins as labels in immunoassays: I. Design and synthesis of flavin labels
899
J.P. Albarella, D.L. Morris and K.F. Yip

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Flavins as labels in immunoassays: II. Properties of flavin labels and their use in immunoassay
903
David L. Morris and James P. Albarella

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Author Index
907

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Subject Index
913

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Backmatter
925

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Publishing information

Pages and Images/Illustrations in book

eBook published on:

April 1, 2019

eBook ISBN:

9783111521350

Hardcover published on:

April 1, 1984

Hardcover ISBN:

9783110098792

Edition:

Reprint 2019

Pages and Images/Illustrations in book

Front matter:

34

Main content:

923

Other:

Num. figs.

https://doi.org/10.1515/9783111521350

eBook ISBN: 9783111521350

Hardcover ISBN: 9783110098792

Keywords for this book

Flavine; Flavoenzym

Creative Commons

BY-NC-ND 4.0

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Manufacturer information:: Walter de Gruyter GmbH
Genthiner Straße 13
10785 Berlin; productsafety@degruyterbrill.com

Flavins and Flavoproteins

Overview

About this book

Topics

Table of contents

Frontmatter

Preface

Organising Committee/Local Committee/Acknowledgements

Contents

Participants

The influence of hydrogen bond formation with the N(l) atom on the orbital structure of flavin

Spectral and photochemical properties of alloxazines

π...π-interactions of flavins : novel coenzyme models of the cyclophane type

A laser flash photolysis study of the triplet states of lumichromes

The dark formation of radicals in flavinium cation/acid systems

ENDOR studies on flavin radicals

On the role of some flavin adducts as one-electron donors

Photoinactivation of flavin redox catalysis: the reductive flavin photoadduct formation

Flavin oxygen chemistry brought to date

Pulse radiolysis studies on the equilibria between reduced and oxidized free flavin species and the effect of molecular oxygen

Effect of pH on the oxidation-reduction properties of 8α - imidazole flavins

Studies of intermediates in reactions of flavins and sulphydryl compounds

A kinetic study on the acid-catalysed phosphate migration in riboflavin phosphates

Chemical structure of nekoflavin

Binding mode and action of FAD in glutathione reductase

Active site chemical modification and sequencing of flavoproteins

Molecular genetic approaches to the study of E. coli flavoproteins

Glutathione reductase: mutation, cloning and sequence analysis of the gene in E. coli

The coenzyme binding site of glutathione reductase. Correlation of X-ray studies with kinetic data

13C-NMR study on the active sites of lipoamide dehydrogenase and glutathione reductase

X-ray crystallographic studies on lipoamide dehydrogenase from Azotobacter vinelandii

Mobility of lipoamide dehydrogenase in and out of the pyruvate dehydrogenase complex from Azotobacter vinelandii

Partial amino acid sequence of pig heart lipoamide dehydrogenase

The amino acid sequence encompassing the active site histidine residue of lipoamide dehydrogenase from Escherichia coli labelled with a bifunctional arsenoxide

Inactivation of pig heart lipoamide dehydrogenase by 1,3-dibromoacetone

The evolution of mercuric reductase, and a redox transfer model for mercuric ion detoxification in bacteria

Structural studies on ferredoxin-NADP+ oxidoreductase from Spirulina, a blue-green alga

The amino acid sequence and partial tertiary structure of ferredoxin-NADP+ oxidoreductase from spinach

On the nature of ferredoxin: ferredoxin-NADP+ reductase complex

Properties of a cross-linked complex between ferredoxin-NADP+ reductase and ferredoxin

On the enigma of old yellow enzyme's spectral properties

"On the enigma of old yellow enzyme's spectral properties"

NMR studies on the old yellow enzyme

Structural and kinetic characteristics of dimethylglycine dehydrogenase and sarcosine dehydrogenase

Evidence for two spatially distinct domains on each subunit of methylenetetrahydrofolate reductase

Structure of NADH-cytochrome b5 reductase of human erythrocytes

Structural comparison of the succinate dehydrogenase and fumarate reductase of Escherichia coli

Lack of assembly of succinate and NADH-ubiquinone oxidoreductases in iron-deficient rat skeletal muscle mitochondria

Crystal structure study of trimethylamine dehydrogenase

The flavin domain of assimilatory NADH: nitrate reductase from Chlorella vulgaris

Polarized absorption spectra of flavocytochrome b2 single crystals

FMN-protein interactions in flavodoxin from A. nidulans

Photochemical formation of a stable red derivative of flavodoxin

Desulfovibrio vulgaris flavodoxin. A 13C and 15N NMR investigation

13C-NMR study on the interaction of riboflavin with riboflavin-binding protein

The structure of glycolate oxidase from spinach

ENDOR studies of flavoproteins

Resonance Raman study on the complexes of D-amino acid oxidase

The role of arginines in D-amino acid oxidase

The effect of the methylation of histidine-217 in pig kidney D-amino acid oxidase on ligand binding and on catalysis

Stoichiometry of the self-association of D-amino acid oxidase

31P NMR and chemical studies on the phosphorus residues in milk xanthine oxidase

Specific modification of NAD+ binding site of chicken liver xanthine oxidase with 5' - p - fluoro - sulphonylbenzoyladenosine

Studies by electron paramagnetic resonance spectroscopy of the environment of the metal in the molybdenum cofactor from xanthine oxidase

Coupling between Mo(V) and reduced Fe/S 1 centres in aldehyde oxidase and xanthine oxidase

Partial amino acid sequence of L - lactate oxidase from M. smegmatis

Chemical modification of sulphydryl groups in p - hydroxybenzoate hydroxylase from Pseudomonas fluorescens

Chemical modification of phenol hydroxylase by p-nitrobenzenes ulphonyl fluoride

Studies of 2,5-diketocamphane monooxygenase from Pseudomonas putida ATCC 17453

Recent progress in bioluminescence: cloning of the structural genes encoding bacterial luciferase, analysis of the encoded sequences, and crystallization of the enzyme

Probing the bacterial luciferase aldehyde site by affinity and photoaffinity labeling

The catalytic turnover of bacterial luciferase produces a quasi-stable species of altered conformation

Electron microscopy and X-ray diffraction studies on heavy riboflavin synthase from Bacillus subtilis

Heavy riboflavin synthase from Bacillus subtilis. Primary structure and reaggregation of the B subunits

Mechanism of α,β-dehydrogenation of fatty acid CoA derivatives by flavin enzymes

Butyryl-CoA dehydrogenase: Aspects of acceptor and substrate specificity

Oxygen reactivity of butyryl-CoA dehydrogenase from Megasphaera elsdenii and from ox liver mitochondria

Suicide inactivation of short-chain acyl-CoA dehydrogenases by propionyl-CoA. Formation of a substrate - flavin adduct

Structure of the flavin N-5 adduct free radical obtained following inhibition of short-chain acyl-CoA dehydrogenase by propionyl-CoA

Purification and properties of five distinct acyl-CoA dehydrogenases from rat liver mitochondria

¹³C-NMR study on the active sites of lipoamide dehydrogenase and glutathione reductase

Structural studies on ferredoxin-NADP⁺ oxidoreductase from Spirulina, a blue-green alga

The amino acid sequence and partial tertiary structure of ferredoxin-NADP⁺ oxidoreductase from spinach

On the nature of ferredoxin: ferredoxin-NADP⁺ reductase complex

Properties of a cross-linked complex between ferredoxin-NADP⁺ reductase and ferredoxin

Structure of NADH-cytochrome b₅ reductase of human erythrocytes

Polarized absorption spectra of flavocytochrome b₂ single crystals

Desulfovibrio vulgaris flavodoxin. A ¹³C and ¹⁵N NMR investigation

¹³C-NMR study on the interaction of riboflavin with riboflavin-binding protein

³¹P NMR and chemical studies on the phosphorus residues in milk xanthine oxidase

Specific modification of NAD⁺ binding site of chicken liver xanthine oxidase with 5' - p - fluoro - sulphonylbenzoyladenosine

Transient kinetics of ferredoxin-NADP⁺ reductase reaction

On the mechanism of inactivation of flavocytochrome b₂ (baker's yeast) by acetylenic substrates

Intermolecular hydrogen transfer during transhydrogenation catalysed by flavocytochrome b₂ and lactate oxidase

Product binding as modulator of flavin redox parameters: a mechanism of activity control in dehydrogenase-e^-transferase?

T-jump investigation of intramolecular electron exchanges in Hansenula anomala yeast flavocytochrome b₂, L-lactate-cytochrome c oxidoreductase

A pulse radiolysis study of flavocytochrome b₂: differences in reactivity with carboxylate radicals between flavin and haem b₂