Flavins and Flavoproteins : Proceedings of the Eighth International Symposium, Brighton, England, July 9-13, 1984 / R. C. Bray, P. C. Engel, S. G. Mayhew.

Author/​Artist
Mayhew, S. G. [Browse]
Format
Book
Language
English
Εdition
Reprint 2019
Published/​Created
  • De Gruyter 1984
  • Berlin ; Boston : De Gruyter, [2019]
  • ©1984
Description
1 online resource (xxix, 923 pages) : illustrations

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Summary note
To celebrate the 270th anniversary of the De Gruyter publishing house, the company is providing permanent open access to 270 selected treasures from the De Gruyter Book Archive. Titles will be made available to anyone, anywhere at any time that might be interested. The DGBA project seeks to digitize the entire backlist of titles published since 1749 to ensure that future generations have digital access to the high-quality primary sources that De Gruyter has published over the centuries.
Bibliographic references
Includes bibliographical references and index.
Source of description
Description based on online resource; title from PDF title page (publisher's Web site, viewed 22. Okt 2019)
Rights and reproductions note
This eBook is made available Open Access under a CC BY-NC-ND 4.0 license:
Language note
In English.
Contents
  • van / Müller, Franz
  • Kinetic mechanism of the reductive half of reaction catalysed by sailcylate hydroxylase / Wang, Lee-Ho / Tu, Shiao-Chun
  • The pH dependence of enzyme-phenol complexes of phenol hydroxylase / Neujahr, Halina Y.
  • Differential induction and characterization of flavoprotein hydroxylases in Pseudomonas cepacia / Hamzah, Riyad Y. / Tu, Shiao-Chun
  • Steroid monoxygenase from Cylindrocarpon radicicola. An FAD-containing Baeyer-Villiger type oxygenase / Itagaki, Eiji / Katagiri, Masayuki
  • Unusual properties of the flavocytochrome p-cresol methylhydroxylase / McIntire, William S. / Koerber, Steven C. / Bohmont, Craig W. / Singer, Thomas P.
  • Identification of the luciferase-bound flavin-4a-hydroxide as the primary emitter in the bacterial bioluminescenee reaction / Kurfürst, Manfred / Hastings, J. Woodland / Ghisla, Sandro / Macheroux, Peter
  • Studies on the bacterial luciferase reaction: isotope effects on the light emission. Is a "CIEEL" mechanism involved? / Macheroux, Peter / Ghisla, Sandro / Kurfürst, Manfred / Hastings, J. Woodland
  • Probes for the active site of bacterial luciferase / McCapra, Frank / Walpole, Christopher S. J. / Street, Ian P.
  • The cellobiose oxidoreductases of Sporotrichum pulverulentum / Morpeth, Fraser F.
  • The equilibration of reducing equivalents within milk xanthine oxidiase / Hille, Russ
  • Reactions between xanthine oxidase and 4-hydroxy-7-azapteridine / Stewart, Richard C. / Massey, Vincent
  • "Type 1" and "Type 2" rapid and slow EPR signals from the molybdenum centres of molybdenum-containing hydroxylases and their significance / Bray, R.C. / George, G.N. / Gutteridge, S. / Morpeth, F.F. / Turner, N.
  • Re-sulphuration of xanthine oxidase / Ventom, A. / Bray, R.C.
  • Reactivation of desulpho-xanthine oxidase by an enzymatic system / Nishino, Takeshi / Usami, Chikako / Tsushima, Keizo
  • The existence of desulpho-xanthine dehydrogenase in rat liver / Ikegami, Tadashi / Nishino, Takeshi / Tsushima, Keizo
  • The structures and catalytic mechanisms of molybdenum centres in enzymes studied by e.p.r and X-ray spectroscopy / Bray, R.C.
  • Biochemistry of naturally-occurring deazaflavin coenzymes / Walsh, Christopher
  • Interaction of the herbicide sulfometuron methyl with acetolactate synthase: a slow-binding inhibitor / Schloss, John V.
  • The rate-determining step in pteridine-dependent monooxygenases is not ring cleavage / Pike, David / Hora, Mary / Bailey, Steven / Ayling, June
  • The one-electron reduction of riboflavin-binding protein / Faraggi, M. / Klapper, Michael H.
  • Modified Flavins in Flavoproteins
  • 8-azidoflavins: photoaffinity labels for flavoproteins / Ghisla, Sandro / Fitzpatrick, Paul F. / Massey, Vincent
  • Glutathione reductase species containing FAD analogues / Krauth-Siegel, R.L. / Schirmer, R.H. / Ghisla, S.
  • Flavin analogue studies of pig kidney electron transferring flavoprotein / Gorelick, Robert J. / Thorpe, Colin
  • Chemically modified flavins as probes of phenol hydroxylase structure and function / Detmer, Kristina / Massey, Vincent
  • 4-thioflavins as active site probes of flavoproteins: reaction with sulphite and formation of 4-hydroxy-4-sulphonylflavins / Claiborne, Al / Massey, Vincent / Biemann, Monika / Ghisla, Sandro
  • Oxygen reactivity of 4-thio-FAD p-hydroxybenzoate hydroxylase / Claiborne, Al / Schopfer, Lawrence M. / Massey, Vincent
  • Oxygen reactions of para-hydroxy benzoate hydroxylase containing 6-hydroxy-FAD / Entsch, Barrie / Massey, Vincent
  • The effect of pH and modifications in position 8 on the oxidation of reduced p-hydroxybenzoate hydroxylase / Schopfer, L.M. / Wessiak, Albert / Massey, Vincent
  • Reaction of bacterial luciferase from Vibrio harveyi with 8-substituted flavins / Chen, Lorenzo / Baldwin, Thomas O.
  • Biomedical Aspects
  • Intestinal absorption of riboflavin / Kasai, Sabu / Nakano, Hideko / Matsukawa, Hirokazu / Miyake, Yoshihiro / Matsui, Kunio
  • Transfer of hydrogen atoms from pentose phosphate to the xylene ring of riboflavin / Keller, P.J. / Floss, H.G. / Le Van, Q. / Neuberger, G. / Nielsen, P. / Bacher, A.
  • Biosynthesis of riboflavin Enzymatic formation of 6,7-dimethyl-8-ribityllumazine / Bacher, A. / Nielsen, P. / Neuberger, G. / Floss, H. G.
  • Cell-free biosynthesis of lipoamide dehydrogenase / Koike, Kichiko / Tsuji, Akihiko / Urata, Yoshishige / Moriyasu, Matsuko / Koike, Masahiko
  • Covalently 14C-riboflavin-labeled proteins in Arthrobacter oxidans and their possible relationship to 6-hydroxy-D-nicotine oxidase / Decker, Karl / Reeves, Henry / Brandsch, Roderich
  • Electron immunochemical localization of 6-hydroxy-nicotine oxidases in Arthrobacter oxidans / Swafford, James R. / Reeves, Henry C. / Brandsch, Roderich / Decker, Karl
  • Cloning in Escherichia coli of the 6-hydroxy-D-nicotine oxidase gene from Arthrobacter oxidans / Brandsch, Roderich
  • Hydroxylation of riboflavin 7- and 8-methyl groups in mammals / Yagi, Kunio / Ohishi, Nobuko / Ohkawa, Hiroshi
  • Mammalian metabolism of flavins / McCormick, D.B. / Innis, W.S.A. / Merrill, A.H. / Lee, S.-S.
  • Flavoenzymes as drug targets / Schirmer, R. Heiner / Lederbogen, Florian / Krauth-Siegel, R. Luise / Eisenbrand, Gerhard / Schulz, Georg / Jung, Albrecht
  • Studies on Esherichia coli photolyase: role of flavin in DNA repair / Schuman Jorns, Marilyn / Sancar, Gwendolyn B. / Sancar, Aziz
  • Electron transfer to nitrogenase in K-pneumoniae nifF gene cloned and the gene product, a flavodoxin, purified and partially characterised / Deistung, J. / Hill, S. / Thorneley, R.N.F. / Cannon, F. / Cannon, M.
  • Practical Applications of Flavoprotein Studies
  • In vitro synthesis of (bio)chemicals using flavin-containing enzymes / Laane, Colja / Hilhorst, Riet / Spruijt, Ruud / Dekker, Koen / Veeger, Cees
  • Flavin cofactors covalently attached to electron-conducting supports: electrochemical and enzyme activity / Wingard, Lemuel B. / Narasimhan, Krishna / Miyawaki, Osato
  • Luminometric determination of immunoadsorbed flavoproteins and of flavin adenine dinucleotide / Hinkkanen, Ari / Decker, Karl
  • Flavins as labels in immunoassays: I. Design and synthesis of flavin labels / Albarella, J.P. / Morris, D.L. / Yip, K.F.
  • Flavins as labels in immunoassays: II. Properties of flavin labels and their use in immunoassay / Morris, David L. / Albarella, James P.
  • Author Index
  • Subject Index
  • Backmatter
  • -- Chemical modification of phenol hydroxylase by p-nitrobenzenes ulphonyl fluoride / Sejlitz, C. Torsten / Neujahr, Halina Y.
  • Studies of 2,5-diketocamphane monooxygenase from Pseudomonas putida ATCC 17453 / Taylor, David G. / Trudgill, Peter W.
  • Recent progress in bioluminescence: cloning of the structural genes encoding bacterial luciferase, analysis of the encoded sequences, and crystallization of the enzyme / Baldwin, Thomas O. / Johnston, Timothy C. / Swanson, Rosemarie
  • Probing the bacterial luciferase aldehyde site by affinity and photoaffinity labeling / Tu, Shiao-Chun / Fried, Aaron
  • The catalytic turnover of bacterial luciferase produces a quasi-stable species of altered conformation / AbouKhair, Nabil K. / Ziegler, Miriam M. / Baldwin, Themas O.
  • Electron microscopy and X-ray diffraction studies on heavy riboflavin synthase from Bacillus subtilis / Ladenstein, Rudolf / Meyer, Birgit / Huber, Robert / Labischinski, Harald / Bartels, Klaus / Bartunik, Hans-Dieter / Bachmann, Luis / Ludwig, Heide C. / Bacher, Adelbert
  • Heavy riboflavin synthase from Bacillus subtilis. Primary structure and reaggregation of the B subunits / Ludwig, Heide C. / Lottspeich, Friedrich / Henschen, Agnes / Ladenstein, Rudolf / Bacher, Adelbert
  • Enzyme Reaction Mechanisms
  • Mechanism of α,β-dehydrogenation of fatty acid CoA derivatives by flavin enzymes / Ghisla, Sandro
  • Butyryl-CoA dehydrogenase: Aspects of acceptor and substrate specificity / Engel, Paul C. / Williamson, Gary / Shaw, Lee
  • Oxygen reactivity of butyryl-CoA dehydrogenase from Megasphaera elsdenii and from ox liver mitochondria / Ellison, Patricia / Shaw, Lee / Williamson, Gary / Engel, Paul C.
  • Suicide inactivation of short-chain acyl-CoA dehydrogenases by propionyl-CoA. Formation of a substrate - flavin adduct / Shaw, Lee / Engel, Paul C.
  • Structure of the flavin N-5 adduct free radical obtained following inhibition of short-chain acyl-CoA dehydrogenase by propionyl-CoA / George, Graham N. / Shaw, Lee / Bray, Robert C. / Engel, Paul C.
  • Purification and properties of five distinct acyl-CoA dehydrogenases from rat liver mitochondria / Ikeda, Yasuyuki / Ikeda, Kazuko O. / Tanaka, Kay
  • Mechanism of action of short-chain, medium-chain and long-chain acyl-CoA dehydrogenases isolated from rat liver / Ikeda, Yasuyuki / Hine, David / Ikeda, Kazuko O. / Tanaka, Kay
  • Inactivation of pig kidney general acyl-CoA dehydrogenase by 2-alkynoyl-CoA derivatives / Freund, Kurt / Mizzer, John P. / Thorpe, Colin
  • On the inactivation of general acyl-CoA dehydrogenase from pig kidney by methylenecyclopropyl-acetyl-CoA, a metabolite of hypoglycin / Zeller, Hans-Dieter / Ghisla, Sandro
  • Structure-function correlation in B-oxidation enzymes / Rojas, Camilo / Gustafson, William / Schmidt, Jack / Domanski, Dan / Feinberg, Benjamin A. / McFarland, James T.
  • Purification and characterization of glutaryl-CoA dehydrogenase, electron transfer flavoprotein and ETF-CoQ oxidoreductase from Paracoccus denitrificans / Husain, Mazhar / Steenkamp, Daniel J.
  • Reactions of ETF and ETF-CoQ oxidoreductase / Steenkamp, D.J. / Ramsay, R.R. / Husain, M.
  • Correlation between redox state of ETF and dehydrogenation of octanoyl-CoA / Hall, Carole L.
  • Some observations on an acrylyl-CoA reductase from Clostridium kluyveri and an NADH-dependent fumarate reductase from Enterobacter agglomerans / Sedlmaier, Helmut / Bühler, Mathias / Feicht, Richard / Bader, Johann / Simon, Helmut
  • Characterization of the mode of electron transport of NADPH-adrenodoxin reductase / Yamano, Toshio / Nonaka, Yasuki / Fujii, Shigeru
  • Studies on forward and reverse reactions of adrenodoxin reductase by electronic and NMR spectroscopy / Nonaka, Y. / Fujii, S. / Yamano, T.
  • Transient kinetics of ferredoxin-NADP+ reductase reaction / Yoshikawa, Shinya / Ohnishi, Norihiro / Morigiwa, Aiko / Takeshima, Katsuhito / Matsumoto, Midori / Nishiyama, Kyoko / Matsubara, Hiroshi / Kodo, Keiun
  • Some new ideas about the possible regulation of redox potentials in flavoprotein, with special reference to flavodoxins / Moonen, Chrit T.W. / Vervoort, Jacques / Müller, Franz
  • Methylenetetrahydrofolate reductase: an imperfect enzyme? / Vanoni, Maria A. / Matthews, Rowena G.
  • Probing the catalytic mechanism of glutathione reductase with 2,4,6-trinitrobenzenesulphonate / Carlberg, Inger / Mannervik, Bengt
  • Multifunctionality of yeast glutathione reductase / Tsai, C.S. / Godin, J.R.P. / Tsai, Y.H.
  • The reaction between NADPH and mercuric reductase / Sahlman, Lena / Lindskog, Sven / Lambeir, Anne-Marie / Dunford, H. Brian
  • Dehydrohalogenation and intermolecular hydrogen transfer reactions catalyzed by some lactate-oxidizing enzymes / Lederer, Florence
  • On the mechanism of inactivation of flavocytochrome b2 (baker's yeast) by acetylenic substrates / Pompon, Denis / Lederer, Florence
  • Intermolecular hydrogen transfer during transhydrogenation catalysed by flavocytochrome b2 and lactate oxidase / Urban, Philippe / Lederer, Florence
  • Product binding as modulator of flavin redox parameters: a mechanism of activity control in dehydrogenase-e-transferase? / Labeyrie, Françoise / Janot, Jean-Marc / Tegoni, Mariella
  • T-jump investigation of intramolecular electron exchanges in Hansenula anomala yeast flavocytochrome b2, L-lactate-cytochrome c oxidoreductase / Tegoni, Mariella / Labeyrie, Françoise / Silvestrini, Maria Chiara / Brunori, Maurizio
  • A pulse radiolysis study of flavocytochrome b2: differences in reactivity with carboxylate radicals between flavin and haem b2 / Capeillère-Blandin, Chantal / Ferradini, Christiane
  • The distribution of reducing equivalents among some species in succinate dehydrogenase upon reduction by succinate / Pagani, Silvia / Bonomi, Franco
  • Ionic species of the flavin and the catalytic cycle of succinate dehydrogenase / Bonomi, Franco / Pagani, Silvia
  • ESR spectroscopic studies of succinate dehydrogenase and fumarate reductase from Escherichia coli / Cammack, Richard / Patil, Daulat S. / Condon, Caro / Owen, Peter / Cole, Stewart T. / Weiner, Joel H.
  • Fumarate reductase from Escherichia coli requires the frdC and frdD gene products for quinone reductase activity / Cecchini, Gary / Ackrell, Brian A. C. / Kearney, Edna B. / Gunsalus, Robert P.
  • Glutamate synthase from Azospirillum brasilense / Ratti, Sabina / Curti, Bruno / Zanetti, Giuliana
  • Oxidation-reduction properties of glycolate oxidase / Pace, Charles / Stankovich, Marian
  • Studies with the flavin-dependent alcohol oxidase from yeast: properties and catalytic mechanism / Geissler, Johanna / Kroneck, Peter M.H. / Ghisla, Sandro
  • Pulse radiolysis studies on the formation and decay of the flavin 4a-hydroperoxide species of glucose oxidase / Anderson, Robert F. / Massey, Vincent / Schopfer, Lawrence M.
  • E.coli pyruvate oxidase: a hysteretic enzyme / Mather, Michael W. / Gennis, Robert B.
  • Mechanism and functionality of FMN in liver pyridoxine (pyridoxamine) 5'-phosphate oxidase / Bowers-Komro, Delores M. / McCormick, Donald B.
  • Enzymatic properties of yeast pyridoxamine-P oxidase / Tsuge, Haruhito / Okada, Toshitaka / Nakane, Izumi / Uchida, Shinji / Sugiyama, Reiko / Ohashi, Kazuji
  • A photo-labelling reagent of brain pyridoxine-5-P oxidase / Churchich, J. E.
  • Non-stereospecific reduction of monoamine oxidase from bovine liver by analogs of amphetamine / Weyler, Walter / Salach, James I. / Coutts, R.T. / Baker, G.B.
  • The kinetics of NADPH-dependent reduction of FAD and cytochrome b in a solubilised preparation of the superoxide generating oxidase of neutrophils / Cross, Andrew / Parkinson, John / Jones, Owen
  • Flavoprotein monooxygenases / Ballou, David P.
  • The nature of the 4a-hydroperoxyflavin in the mammalian flavin-containing monooxygenase / Jones, Kenneth / Ballou, David P.
  • 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 / Wijnands, Robert A. / Leeuwen, Johan W. van / Berkel, Willem J.H.
  • Frontmatter
  • Preface / Bray, R.C. / Engel, P.C. / Mayhew, S.G.
  • Organising Committee/Local Committee/Acknowledgements
  • Contents
  • Participants
  • Flavin Chemistry
  • The influence of hydrogen bond formation with the N(l) atom on the orbital structure of flavin / Müller, Franz / Eweg, Jan Kees / Szczesna, Viola / Hesper, Ben
  • Spectral and photochemical properties of alloxazines / Kozioł, Jacek / Koziołowa, Anna / Babś, Wojciech / Dawidowski, Jan / Panek-Janc, Danuta / Stroińska, Małgorzata / Szczęsna, Violetta / Szymusiak, Henryk / Tyrakowska, Bożena
  • π...π-interactions of flavins : novel coenzyme models of the cyclophane type / Zipplies, Matthias F. / Staab, Heinz A.
  • A laser flash photolysis study of the triplet states of lumichromes / Heelis, Paul F. / Phillips, G. O.
  • The dark formation of radicals in flavinium cation/acid systems / Addink, R. / Mager, H.I.X.
  • ENDOR studies on flavin radicals / Bock, Michael / Elsner, Martin / Kurreck, Harry
  • On the role of some flavin adducts as one-electron donors / Mager, H.I.X. / Addink, R.
  • Photoinactivation of flavin redox catalysis: the reductive flavin photoadduct formation / Ott, Ulrich / Traber, Rainer / Kramer, Horst E.A.
  • Flavin oxygen chemistry brought to date / Bruice, Thomas C.
  • Pulse radiolysis studies on the equilibria between reduced and oxidized free flavin species and the effect of molecular oxygen / Anderson, Robert F.
  • Effect of pH on the oxidation-reduction properties of 8α - imidazole flavins / Williamson, Gary / Edmondson, Dale E.
  • Studies of intermediates in reactions of flavins and sulphydryl compounds / Surdhar, P.S. / Armstrong, D.A.
  • A kinetic study on the acid-catalysed phosphate migration in riboflavin phosphates / Nielsen, Peter / Rauschenbach, Peter / Bacher, Adelbert
  • Chemical structure of nekoflavin / Matsui, Kunio / Kasai, Sabu
  • Flavoprotein Structure
  • Binding mode and action of FAD in glutathione reductase / Schulz, G.E.
  • Active site chemical modification and sequencing of flavoproteins / Williams, Charles H. / Arscott, L. David / Swenson, Richard P.
  • Molecular genetic approaches to the study of E. coli flavoproteins / Guest, J. R. / Rice, D. W.
  • Glutathione reductase: mutation, cloning and sequence analysis of the gene in E. coli / Greer, Shaun / Perham, Richard N.
  • The coenzyme binding site of glutathione reductase. Correlation of X-ray studies with kinetic data / Pai, Emil F. / Horn, Elke / Schulz, Georg E.
  • 13C-NMR study on the active sites of lipoamide dehydrogenase and glutathione reductase / Berg, Willy A.M. van den / Vervoort, Jacques / Moonen, Chrit T.W. / Müller, Franz / Carlberg, Inger / Mannervik, Bengt
  • X-ray crystallographic studies on lipoamide dehydrogenase from Azotobacter vinelandii / Schierbeek, A.J. / Drenth, J. / Hol, W.G.J.
  • Mobility of lipoamide dehydrogenase in and out of the pyruvate dehydrogenase complex from Azotobacter vinelandii / Kok, Arie de / Visser, Antonie J.W.G.
  • Partial amino acid sequence of pig heart lipoamide dehydrogenase / Arscott, L. David / Berman, Martin / Williams, Charles H.
  • The amino acid sequence encompassing the active site histidine residue of lipoamide dehydrogenase from Escherichia coli labelled with a bifunctional arsenoxide / Holmes, Charles F.B. / Stevenson, Kenneth J.
  • Inactivation of pig heart lipoamide dehydrogenase by 1,3-dibromoacetone / Lee, James S. / Williams, Charles H.
  • The evolution of mercuric reductase, and a redox transfer model for mercuric ion detoxification in bacteria / Brown, Nigel L. / Goddette, Dean
  • Structural studies on ferredoxin-NADP+ oxidoreductase from Spirulina, a blue-green alga / Wada, Keishiro / Yao, Yoshio / Tamura, Toshiaki / Matsubara, Hiroshi / Kodo, Keiun
  • The amino acid sequence and partial tertiary structure of ferredoxin-NADP+ oxidoreductase from spinach / Karplus, P. Andrew / Herriott, Jon R. / Walsh, Kenneth A.
  • On the nature of ferredoxin: ferredoxin-NADP+ reductase complex / Shin, Masateru / Sakihama, Naoko
  • Properties of a cross-linked complex between ferredoxin-NADP+ reductase and ferredoxin / Zanetti, Giuliana / Curti, Bruno
  • On the enigma of old yellow enzyme's spectral properties / Eweg, Jan K. / Müller, Franz / Berkel, Willem J.H. van / Hesper, Ben
  • "On the enigma of old yellow enzyme's spectral properties" / Massey, V. / Schopfer, L. M. / Dunham, W. R.
  • NMR studies on the old yellow enzyme / Beinert, Wolf-Dieter / Rüterjans, Heinz / Müller, Franz
  • Structural and kinetic characteristics of dimethylglycine dehydrogenase and sarcosine dehydrogenase / Cook, Robert J. / Porter, David H. / Misono, Kunio S. / Wagner, Conrad
  • Evidence for two spatially distinct domains on each subunit of methylenetetrahydrofolate reductase / Matthews, Rowena G. / Vanoni, Maria A. / Khani, Shahrokh / Hainfeld, James F. / Wall, Joseph
  • Structure of NADH-cytochrome b5 reductase of human erythrocytes / Yubisui, Toshitsugu / Miyata, Toshiyuki / Iwanaga, Sadaaki / Tamura, Minoru / Yoshida, Satoshi / Takeshita, Masazumi
  • Structural comparison of the succinate dehydrogenase and fumarate reductase of Escherichia coli / Guest, J. R. / Darlison, M. G. / Wilde, R. J. / Wood, D.
  • Lack of assembly of succinate and NADH-ubiquinone oxidoreductases in iron-deficient rat skeletal muscle mitochondria / Ackrell, Brian A.C. / Cochran, Bruce / Larson, Kent / Kearney, Edna B. / Maguire, John J. / Dallman, Peter R.
  • Crystal structure study of trimethylamine dehydrogenase / Mathews, F. Scott / Lim, Louis W. / Shamala, N.
  • The flavin domain of assimilatory NADH: nitrate reductase from Chlorella vulgaris / Solomonson, Larry P. / Barber, Michael J.
  • Polarized absorption spectra of flavocytochrome b2 single crystals / Mozzarelli, Andrea / Tegoni, Mariella / Rossi, Gian Luigi
  • FMN-protein interactions in flavodoxin from A. nidulans / Ludwig, Martha L. / Pattridge, Katherine A. / Tarr, George
  • Photochemical formation of a stable red derivative of flavodoxin / Mayhew, Stephen G. / Massey, Vincent
  • Desulfovibrio vulgaris flavodoxin. A 13C and 15N NMR investigation / Vervoort, Jacques / Müller, Franz / LeGall, Jean / Bacher, Adelbert / Sedlmaier, Helmut
  • 13C-NMR study on the interaction of riboflavin with riboflavin-binding protein / Miura, Retsu / Tojo, Hiromasa / Fujii, Shigeru / Yamano, Toshio / Miyake, Yoshihiro
  • The structure of glycolate oxidase from spinach / Lindqvist, Ylva / Brändén, Carl-Ivar
  • ENDOR studies of flavoproteins / Bretz, Norbert / Kurreck, Harry
  • Resonance Raman study on the complexes of D-amino acid oxidase / Nishina, Yasuzo / Shiga, Kiyoshi / Miura, Retsu / Tojo, Hiromasa / Miyake, Yoshihiro / Yamano, Toshio / Watari, Hiroshi
  • The role of arginines in D-amino acid oxidase / Simonetta, Mirella P. / Galliani, Stefania / Vanoni, Maria A. / Ronchi, Severino / Curti, Bruno
  • The effect of the methylation of histidine-217 in pig kidney D-amino acid oxidase on ligand binding and on catalysis / Swenson, Richard P. / Williams, Charles H. / Massey, Vincent
  • Stoichiometry of the self-association of D-amino acid oxidase / Tojo, Hiromasa / Horiike, Kihachiro / Shiga, Kiyoshi / Nishina, Yasuzo / Watari, Hiroshi / Yamano, Toshio
  • 31P NMR and chemical studies on the phosphorus residues in milk xanthine oxidase / Edmondson, Dale E. / Davis, Michael D. / Müller, Franz
  • Specific modification of NAD+ binding site of chicken liver xanthine oxidase with 5' - p - fluoro - sulphonylbenzoyladenosine / Nishino, Tomoko / Nishino, Takeshi / Tsushima, Keizo
  • Studies by electron paramagnetic resonance spectroscopy of the environment of the metal in the molybdenum cofactor from xanthine oxidase / Hawkes, T.R. / Bray, R.C.
  • Coupling between Mo(V) and reduced Fe/S 1 centres in aldehyde oxidase and xanthine oxidase / George, Graham N.
  • Partial amino acid sequence of L - lactate oxidase from M. smegmatis / Giegel, David A. / Massey, Vincent / Williams, Charles H.
  • Chemical modification of sulphydryl groups in p - hydroxybenzoate hydroxylase from Pseudomonas fluorescens / Berkel, Willem J.H. van / Müller, Franz / Weijer, Wicher J. / Jekel, Peter A. / Beintema, Jaap J.
ISBN
3-11-152135-4
OCLC
1102793721
Doi
  • 10.1515/9783111521350
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