Flavins and Flavoproteins 1996

Flavins and Flavoproteins 1996

K.J. Stevenson, V. Massey, C.H. Williams, Jr., editors

ISBN 1895176948
$125.00 hardcover
6.5 x 9.5 in.
August 1997

xxii + 976 pages
Tables, figures, biblios.

About the Book

This publication, a collection of 174 papers, encompasses the fundamental and intricate photochemistry and electron transfer of flavins and flavoproteins, the mechanisms associated with enzymes utilizing flavins (such as dehydrogenases, reductases, oxidases, monooxygenases, synthases, peroxidases), the three-dimensional structures of flavoproteins and flavoenzymes and the emerging role of flavins and flavoproteins in medicine.

Flavins and Flavoproteins 1996 continues the series which has appeared every three years since 1965. Presented are overviews of key areas of flavin research, coupled with the most recent understanding of the chemistry/photochemistry of flavins and the structure/function relationship of numerous proteins/enzymes that use flavins as essential cofactors.

Key Features:

Detailed studies on the structure and mechanism of flavoenzymes are reported together with newly discovered medical aspects
New research of high quality with extensive data, figures and bibliographies
The interaction of flavins with other electron carriers such as the cytochromes, metals, and non-heme iron centres is investigated with a variety of spectrophotometric techniques
NMR and crystallography studies have provided new three-dimensional structures of several flavoenzymes and flavoproteins
Numerous papers on an extensive number of flavoenzymes and complex flavoproteins are presented

Table of Contents

A. Flavins and Flavoproteins in Medicine
K. Becker, M.A. Keese, S. Gromer and R.H. Schirmer	Flavins in medicine. An update	3
K. Becker, P.M. Färber, C-W. von der Lieth and S. Müller	Glutathione reductase and thioredoxin reductase of the malarial parasite Plasmodium falciparum	13
D.E. Edmondson	Structure-activity relationships as probes of the structure and mechanism of monoamine oxidase B	23
R.L. Krauth-Siegel, E.M. Jacoby, M.C. Jockers-Scherübl, I. Schlichting and J. Barbe	T. cruzi trypanothione reductase: Structure-function relationships of enzyme-inhibitor complexes	35
R. Rozen	Methylenetetrahydrofolate reductase deficiency: Risk factor for heart disease and neural tube defects	45
A.W. Segal and K.P. Shatwell	The NADPH oxidase of phagocytes, a flavocytochrome b electron transport chain important in immunity	55
K. Yagi, N. Ohishi, S. Komura and L. Ernster	DT-Diaphorase and Xenobiotics	65
J.R. Miller and D.E. Edmondson	Effect of flavin structure on the enzymatic activity of recombinant human liver monoamine oxidase A	71
B.J. Brown and V. Massey	The effect of mutation of His-191 and Asn-194 on the properties of old yellow enzyme	77
J. Buckman, S.M. Miller, P. Malloy and D. Feldman	Properties of an estrogen binding protein from Candida albicans - a homolog of old yellow enzyme	81
A.R. Krapp, N. Cortez, J.F. Palatnik, V.B. Tognetti, E.M. Valle and N. Carrillo	Les liaisons dangereuses: The flavoprotein ferredoxin-NADP+ reductase as propagator and scavenger of toxic oxygen derivatives	85
A. Otto, R. Brandsch, K. Frenzer-Welle and N. Freudenberg	Tissue specific expression of dimethylglycine dehydrogenase in humans and its presence as antigen to mitochondrial autoantibodies in heart diseases	89
D. Salazar, L. Zhang and F.E. Frerman	Expression and characterization of pathogenic mutations and a bY16L mutation in human electron transfer flavoprotein	93
Y. Tang and T.D. Porter	Cloning of human squalene epoxidase	97
B. Theoretical and Chemical Approach
M. S. Jorns	Role of flavoproteins in light-dependent reactions	103
P. Macheroux, S. Bornemann and R.N.F. Thorneley	Role of reduced FMN in the catalytic mechanism of chorismate synthase	113
E. Breinlinger, A. Niemz and V. Rotello	Synthetic models for flavoenzyme activity: Modification of flavin redox properties through hydrogen bonding	123
Y.E. Bruggeman, W.R. Mulder, A.J.W.G. Visser, C. Laane, R. Hilhorst and A. Schots	Accelerated oxidation of dihydroflavoquinone by a flavin-binding antibody	127
S. Chakraborty, Y.V.S.N. Murthy and V. Massey	Reaction of reduced flavin with diphenyliodonium chloride	131
S. Fujii, K. Kuroda, M. Nakagawa and R. Miura	C13 and F19 NMR studies of old yellow enzyme	135
C.E. Hanine-Lmoumene, L. Lindqvist, F. Lederer and R. Serbanescu	Fast evolution of the pKa of protein-bound flavin semiquinone generated photochemically using UV laser irradiation	139
K. Higashimura, K. Nishimoto, N. Ohishi and K. Yagi	Electronic structures and Geometries of 10-methyl-N(5)H isoalloxazine 4a-hydroperoxide and 10-methyl-N(1)H isoalloxazine 10a-hydroperoxide. Models of flavin hydroperoxides	143
G. Gadda and P.F. Fitzpatrick	Characterization of the flavin adduct of nitroalkane oxidase	147
H.I.X. Mager and S-C. Tu	Electron transfer studies. Disproportionation of flavinium cations and derived flavin radicals	151
K. Matsui and S. Kasai	Photoisomerization of diacetone riboflavin	155
A. Niemz and V. Rotello	UV/Vis spectroelectrochemistry of flavins in aprotic organic solvents	159
R.E. Sharp, F. Rabanal and P.L. Dutton	Design, synthesis and characterisation of a flavocytochrome molecular maquette	163
A.J.W.G. Visser, A. van Hoek, P. Macheroux and R.N.F. Thorneley	Time-resolved fluorescence of substrate induced FMN-binding to chorismate synthase	167
Y. Yano, T. Kajiki and H. Ohshiro	Regulation of flavin functions by artifical receptors via hydrogen bonding	171
C. Oxidases
1. Amino Acid Oxidases
F. Todone, A. Mattevi, M.A. Vanoni and B. Curti	Crystal structure of D-amino acid oxidase	177
S. Ghisla, L. Pollegioni, W. Blodig and M.S. Pilone	On the mechanism of D-amino acid oxidase: Structure/reactivity studies using p-substituted phenylglycines	187
P.F. Fitzpatrick, J.M. Denu and J.J. Emanuele, Jr.	Evidence for rate-limiting conformational changes during the D-amino acid oxidase reaction	195
K. Fukui, T. Kanamori, O. Jinnouchi and O. Ben-Yoseph	Tissue specific expression of the D-amino acid oxidase gene	199
R. Konno, A. Niwa, M. Sasaki, J. Enami, S. Asakura and K. Fukui	Is there D-amino acid oxidase in the mouse liver?	203
H. Mizutani, I. Miyahara, K. Hirotsu, Y. Nishina, K. Shiga, C. Setoyama and R. Miura	Crystal structure of porcine kidney D-amino acid oxidase. Analysis of enyzme-substrate (analog) interaction	207
A. Negri, G. Tedeschi, M. Mortarino, T. Simonic and S. Ronchi	Alternative electron acceptors for L-aspartate oxidase under anaerobic condition. I. L-Asparate:fumarate oxidoreductase activity	211
G. Tedeschi, A. Negri, M. Mortarino, F. Ceciliani and S. Ronchi	Alternative electron acceptors for L-aspartate oxidase under anaerobic condition. II. L-Asparate:quinone oxidoreductase activity	215
Y. Nishina, K. Sato, K. Shiga and R. Miura	Structural modulation of ligand by its binding to reduced D-amino acid oxidase	219
M.S. Pilone and L. Pollegioni	D-amino acid oxidase from Rhodotorula gracilis as a biocatalyst	223
L. Pollegioni, S. Campaner, G. Molla, E. Martegani and M.S. Pilone	Cloning and expression of E. coli of D-amino acid oxidase gene from Rhodotorula gracilis	227
A.A. Raibekas and V. Massey	Glycerol as a chemical chaperone: Model studies utilizing Crotalus adamanteus L-amino acid oxidase	231
M.A. Wagner, A. Willie and M.S. Jorns	Comparison of monomeric and heterotetrameric sarcosine oxidases	235
2. NAD(P)H Oxidase
M. Higuchi	Two types of NADH oxidases induced in Streptoccocus mutans	241
Y. Nisimoto, N. Kawai, J.L.R. Freeman, D.J. Uhlinger and D.L. Lambeth	Rac-effector interaction regulating NADPH oxidase activation	245
3. Other Oxidases
T. Kurihara, N. Gorlatova, M. Tchórzewski, N. Esaki and K. Soda	Nitroalkane-oxidizing enzymes	251
M.W. Fraaije, F. Drijfhout, G.H. Meulenbeld, W.J.H. van Berkel and A. Mattevi	Vanillyl-alcohol oxidase from Penicillium simplicissimum : Reactivity with p-cresol and preliminary structural analysis	261
D. Parsonage and A. Claiborne	Cloning and expression of Enterococcal a-glycerophosphate oxidase	265
S. Schenk and K. Decker	Molecular and preliminary crystallographic investigation of the enantiomer-specific 6-hydroxy-L-nicotine oxidase	269
M. Stoltz, A.F. Bückmann and R. Brandsch	Covalent binding of N6-(2-aminoethyl)-FAD and N6-(6-carboxyhexyl)-FAD to 6-hydroxy-D-nicotine oxidase apoenzyme and mitochondrial import of the flavinylated proteins	275
D. Monooxygenases
1. General Overview
J. Vervoort, L. Ridder, W.J.H. van Berkel and I.M.C.M. Rietjens	Flavoprotein monooxygenases: Mechanistic overview	281
2. p-Hydroxybenzoate Hydroxylase
B.A. Palfey, M. Kasimova, G.R. Moran, B. Entsch, D.P. Ballou and V. Massey	Energetic factors controlling the flavin conformation in p-hydroxybenzoate hydroxylase and their importance in the reduction reaction	295
W.J.H. van Berkel, M.H.M. Eppink, F.J.T. van der Bolt, J. Vervoort, I.M.C.M. Rietjens and H.A. Schreuder	p-Hydroxybenzoate hydroxylase: Mutants and mechanism	305
M.H.M. Eppink, D. Jacobs and W.J.H. van Berkel	Involvement of His162 in NADPH binding of p-hydroxybenzoate hydroxylase	315
B. Entsch, G.R. Moran, D.L. Waters, B.A. Palfey and D.P. Ballou	The influence of charge upon catalysis by p-hydroxybenzoate hydroxylase as found from the study of specific mutants	319
M. Ortiz-Maldonado, D.P. Ballou and V. Massey	Leaving group tendencies of 8-substituted flavin-C4a-alkoxides and the mechanism of hydroxylation catalyzed by p-hydroxybenzoate hydroxylase	323
L. Ridder, J. Vervoort, W.J.H. van Berkel, C. Veeger and I.M.C.M. Rietjens	Molecular orbital analysis of the reaction pathway for hydroxylation of p-hydroxybenzoate by the flavin (C4a)-hydroperoxide intermediate of p-hydroxybenzoate hydroxylase	327
F.J.T. van der Bolt, S. Boeren, J. Vervoort and W.J.H. van Berkel	Reactivity of p-hydroxybenzoate hydroxylase with 2-chloro-4-hydroxybenzoate	331
3. Phenol Hydroxygenases
C. Enroth, Y. Lindqvist, G. Schneider, S. Waters and H. Neujahr	Crystallisation and preliminary X-ray analysis of phenol hydroxylase from Trichosporon cutaneum	337
W.J.H. van Berkel, E. Cammaart, M.H.M. Eppink and J. Vervoort	Purification and properties of phenol hydroxylase from the Ascomycetous yeast Candida parapsilosis	341
4. Luciferase
T.O. Baldwin, M.M. Ziegler, A.C. Clark, J.F. Sinclair, F.M. Raushel, I. Rayment, H.M. Holden, A.J. Fisher, T.B. Thompson and J.B. Thoden	Structure and folding of bacterial luciferase	347
S-C. Tu, B. Lei, Y. Yu and M. Liu	Characterization of Vibrio harveyi NADPH:FMN oxidoreductase and mechanism of reduced flavin transfer to luciferase	357
S. Kasai	Evidence that FP390, the final product of the lux operon in luminous bacteria, has flavodoxin function and takes part in biosynthesis of methionine	367
5. Other Monooxygenases
D. Becker, T. Schräder and J.R. Andreesen	Pyrrole-2-carboxylate monooxygenase from Rhodococcus sp. belongs to the new type of two-component flavin aromatic monooxygenases	375
P. Chaiyen, D.P. Ballou and V. Massey	2-Methyl-3-hydroxypyridine-5-carboxylic acid (MHPC) oxygenase: The hydroxylase capable of catalysing a ring cleavage reaction	379
W.A. Suske, H-P.E. Kohler, M. Held, M.G. Wubbolts and A. Schmid	2-Hydroxybiphenyl 3-monooxygenase, a novel member of the group of FAD-containing aromatic hydroxylases	383
K. Suzuki, M. Mizuguchi, K. Ohnishi and E. Itagaki	Structure of salicylate hydroxylase of Pseudomonas putida S-1: Cloning and sequencing of chromosomal DNA of the enzyme	387
M. Tsujita, R-F. Wu, S. Tomita and Y. Ichikawa	An essential amino acid sequence of the substrate (amine)-binding region of porcine FAD-containing monooxygenase	391
H. Tsuji, T. Oka, M. Kimoto, T. Ogawa, T. Sasakawa and K. Sato	Cloning and sequencing of cDNA encoding 4-amino-benzoate hydroxylase from Agaricus bisporus	395
W.J.H. van Berkel, K. Ruiter, M.H.M. Eppink and J. Vervoort	Substrate specificity of 4-hydroxybenzoate 1-hydroxylase from Candida parapsilosis	399
L. Xi, J.D. Childs, D.J. Monticello and C.H. Squires	Production of DszC oxygenase in Escherichia coli produces indigo	403
E. Electron Transferases
1. Flavodoxins
M.L. Ludwig, K.A. Pattridge, A.L. Metzger, M.M. Dixon, M. Eren, Y. Feng and R.P. Swenson	Oxidation-reduction linked conformation changes and control of potentials in flavodoxin from Clostridium beijerinckii	409
H. Rüterjans, M. Blümel, A. Hrovat, F. Löhr and S.G. Mayhew	Refined solution structure and backbone dynamics of Desulfovibrio vulgaris Flavodoxin	419
R.P. Swenson and Z. Zhou	Role of electrostatic interactions in the regulation of the one-electron reduction potentials in the Desulfovibrio flavodoxin	427
S.M. Geoghegan and S.G. Mayhew	Effects of changing the surface glutamate-14 to lysine on the properties of flavodoxin from Megasphaera elsdenii	437
M. Kitamura, M. Taniguchi, T. Nakaya, T. Sagara and H. Akutsu	Cloning and expression of the flavodoxin gene from Desulfovibrio vulgaris (Miyazaki F)	441
C.T. Sharkey, S.G. Mayhew, T.M. Higgins and M.A. Walsh	Crystallographic studies on flavodoxin from Megasphaera elsdenii	445
C.P.M. van Mierlo, E. Steensma, W.M.A.M. van Dongen and W.J.H. van Berkel	NMR studies on apoflavodoxin II from Azotobacter vinelandii	449
2. P-450 Reductases
J-J.P. Kim, M. Wang, D.L. Roberts, R. Paschke, T. Shea and B.S.S. Masters	How do two flavins communicate with each other? The three-dimensional structure of NADPH-cytochrome P450 reductase	455
A. Aliverti and G. Zanetti	Intramolecular electron transfer within a chimeric iron-sulfur flavoprotein	463
A.W. Munro, R.M. Cook, J.G. Lindsay, J.R. Coggins, S. Daff and S.K. Chapman	Kinetic analysis of P-450 BM3 from Bacillus megaterium	467
H. Otsuka-Murakami, K. Takeya and Y. Nisimoto	NADPH-cytochrome P-450 reductase-like flavoprotein from human granulocyte: Purification, characterization and molecular cloning	471
I. Sevrioukova, J.A. Peterson and D.P. Ballou	Studies of the flavoprotein domain of cytochrome P450BM3	475
Y. Tang and T.D. Porter	Deletion analysis of the FAD domain of NADPH-cytochrome P450 reductase	479
P. Urban and D. Pompon	Cloning and characterization of two arabidopsis NADPH-cytochrome P450 reductase isoforms	483
3. Ferrodoxin-NADP+ Reductases
J.K. Hurley, G. Tollin, M. Fillat, C. Genzor and C. Gómez-Moreno	Anabaena ferredoxin/ferredoxin NADP+ reductase: Role of electrostatic and hydrophobic interactions in complexation and electron transfer	489
V. Nivière, F. Fieschi, C. Frier, J-L. Décout and M. Fontecave	Is the flavin reductase of Escherichia coli a member of the ferredoxin:NADP+ reductase family? Identification of an essential amino acid residue involved in flavin binding and catalysis	497
J. Ottado, N.B. Calcaterra, A.K. Arakaki, E.G. Orellano, N. Carrillo and E.A. Ceccarelli	On the role of aromatic amino acids interacting with FAD in plant-type ferredoxin-NADP+ reductases	501
K. Wada, M. Tsumura, K. Aoki, S. Morigasaki , W. Katoh, K. Yamaguchi and T. Jin	Structure and function of root-type ferredoxin NADP+ reductase	505
G. Zanetti, A. Aliverti, D. Ravasi, B. Curti, Z. Deng and P. Karplus	On the role of glutamate 312 of spinach ferrdoxin-NADP+ reductase	509
4. Electron Transfer Flavoprotein
R.P. Swenson and D. Chen	Nucleotide-binding properties of the recombinant W3A1 electron transferring flavoprotein	515
T.M. Dwyer, K.J. Griffin and F.E. Frerman	Investigation of the aT244M mutation in Paracoccus denitrificans electron transfer flavoprotein	519
D.L. Roberts, F.E. Frerman and J-J.P. Kim	Human electron transfer flavoprotein: Three dimensional structure and a possible complex with medium chain acyl-CoA dehydrogenase	523
5. Other
K. Miki and H. Nishida	Crystal structure of NADH-cytochrome b5 reductase	529
H.J. Lee, L-Y. Lian and N.S. Scrutton	Rubredoxin and rubredoxin reductase of Pseudomonas oleovorans : A model system for investigating interprotein electron transfer	539
F. a-Hydroxyacid Oxidation
F. Lederer	The mechanism of flavoprotein-catalyzed a-hydroxy acid dehydrogenation, revisited	545
C. Bell, S. Uhrinova, P.N. Barlow, S.K. Chapman and G.A. Reid	Domain Mobility in flavocytochrome b2: Fact or fiction	555
A. Filipe, A. Belmouden, J-M. Lacombe and F. Lederer	Long-chain a-hydroxy acid oxidase: Substitution of the active site Phe23 with tyrosine	559
E.H.J. Gordon, S.L. Pealing, S.K. Chapman, F.B. Ward and G.A. Reid	Expression of recombinant flavocytochrome c in Shewanella putrefaciens	563
I. Lehoux and B. Mitra	Mutagenesis studies of active site residues of (S)-mandelate dehydrogenase from Pseudomonas putida	567
A.D. Pike, S.K. Chapman, F.D.C. Manson, G.A. Reid, M. Gondry and F. Lederer	Investigating the importance of an interface residue in interdomain electron transfer	571
D.M. Short, M.D. Walkinshaw, P. Taylor, G.A. Reid and S.K. Chapman	The cytochrome c recognition site on flavocytochrome b2	575
R. Sinclair, G.A. Reid, S. Daff and S.K. Chapman	Constructing a mandelate dehydrogenase	579
W. Sun, C.H. Williams, Jr. and V. Massey	L-Lactate monooxygenase from Mycobacterium smegmatis : Site-directed mutagenesis of glycine 99	583
F.E. Welsh, L. Kohler, S.L. Rivers, G.A. Reid and S.K. Chapman	Forced evolution of cytochrome c recognition site on the flavin domain of flavocytochrome b2	587
K. Yorita, K. Aki, T. Ohkuma-Soyejima, T. Kokubo, H. Misaki and V. Massey	Conversion of L-lactate oxidase to a long chain L-a-hydroxyacid oxidase by replacement of Ala-95 to Gly	591
G. Acyl Coenxyme A Oxidation
C. Thorpe, R.A. Schaller, A-W.A. Mohsen and J. Vockley	The acyl-CoA dehydrogenases: Some mechanistic aspects	597
D.K. Srivastava, J.K. Johnson, N.R. Kumar and K.L. Peterson	Molecular basis for the origin of the "oxidase" activity in medium chain acyl-CoA dehydrogenase	605
H. Tamaoki, C. Setoyama, R. Miura, I. Hazekawa, Y. Nishina and K. Shiga	Spectroscopic study of two forms of rat acyl-CoA oxidase	615
A. Djebli, Y.H. Song, E.F. Pai and U. Eikmanns	Crystallographic studies of the green flavoenzyme 5-hydroxyvaleryl-CoA dehydratase - dehydrogenase from Clostridium aminovalericum	625
S. Ghisla, A. Braunwarth and P. Vock	pH and substrate chain length dependence of the activity of "short-chain"-, "medium-chain"- and "long-chain"- acyl-CoA dehydrogenase	629
N.R. Kumar, K.L. Peterson and D.K. Srivastava	Probing the rate limiting step of the medium-chain acyl-CoA dehydrogenase catalyzed reaction utilizing octanoyl-CoA as a physiological substrate	633
G.J. Mancini-Samuelson, M.T. Stankovich, P. Vock, V. Kieweg and S. Ghisla	Probing the electron transfer properties of human medium-chain acyl-CoA dehydrogenase and site-directed mutants	637
K.L. Peterson, W. Gu and D.K. Srivastava	Recombinant human liver medium chain acyl-CoA dehydrogenase: Functional role of the 3'-phosphate group of acyl-CoA substrates during the enzyme catalysis	641
K.M. Sabaj, M.T. Stankovich and V. Anderson	Exploring the redox properties of MCAD bound to two analogs, acetoacetyl-CoA and hexadienoyl-CoA	645
K.A. Tiffany, M. Wang, R. Paschke, A-W.A. Mohsen, J. Vockley and J-J.P. Kim	Structural basis for substrate specificity in acyl-CoA dehydrogenases: What makes isovaleryl-CoA dehydrogenase specific for a branched chain substrate?	649
H. Flavoprotein Disulfide Reductases
1. Dihydrolipoamide Dehydrogenase
M. Conner and J.G. Lindsay	Biochemical characterisation of a distinct dihydrolipoamide dehydrogenase from pea chloroplasts	655
R.M. Cook, A.W. Munro and J.G. Lindsay	Distinct forms of the FAD containing protein dihydrolipoamide dehydrogenase (E3) are found in tubers and leaves of potato (Solanum tuberosum)	659
J. Marcinkeviciene and J.S. Blanchard	Mycobacterial lipoamide dehydrogenase: Purification and kinetic properties	663
A.H. Westphal, A. de Kok, D.A.A. Ala'Aldeen, M. Atta and M. Veenhuis	Lipoamide dehydrogenase from Neisseria meningitidis	667
D. Ward, A. Claiborne, A. de Kok and A.H. Westphal	Functional and regulatory studies on two distinct lipoamide dehydrogenases from Enterococcus faecalis	673
2. Glutathione Reductase
L.D. Arscott, D.M. Veine and C.H. Williams, Jr.	Mixed disulfide is an observed intermediate in the reaction of glutathione reductase (EH2) with glutathione	679
A.R. Frank and K.J. Stevenson	Bis-g-glutamylcystine reductase from Halobacterium halobium	683
A. Nordhoff, K. Becker, R.H. Schirmer, C. Tziatzios, J.A. van den Broek and D. Schubert	Denaturation and reactivation of dimeric human glutathione reductase	687
A. Nordhoff, S. Gromer, M. Tutic, R.H. Schirmer, C. Granzow and D. Werner	Mouse glutathione reductase of Ehrlich ascites tumour cells	693
P.A.W. van den Berg, A. van Hoek, A.J.W.G. Visser, C.D. Walentas and R.N. Perham	Time-resolved flavin fluorescence quenching in E. coli glutathione reductase	697
3. Thioredoxin Reductase
B.W. Lennon, D.M. Veine, P-F. Wang, S.B. Mulrooney and C.H. Williams, Jr.	Thioredoxin reductase: Structure and Mechanism	703
B.W. Lennon, C.H. Williams, Jr., and M.L. Ludwig	Crystallization of stable mixed disulfides of E. coli thioredoxin reductase and thioredoxin	713
S.B. Mulrooney and C.H. Williams, Jr.	Evidence for two conformational states of thioredoxin reductase: Fluorescence studies of treated and untreated C138S mutant	717
D.M. Veine and C.H. Williams, Jr.	Re-evaluation of the active site mutant C138S from E. coli thioredoxin reductase	721
P-F. Wang, B.W. Lennon and C.H. Williams, Jr.	Reduction of a covalent complex between thioredoxin reductase and its substrate thioredoxin by NADPH	725
4. Peroxide Reductases
A. Claiborne, E.J. Crane,III, D. Parsonage, J.I. Yeh, W.G.J. Hol and J. Vervoort	NADH peroxidase from Enterococcus faecalis: Crystal structure, 13C NMR analysis, and mechanism	731
Y. Niimura, K. Ohnishi, Y. Nishiyama, S. Kawasaki, T. Miyaji, H. Suzuki, T. Nishino and V. Massey	Amphibacillus xylanus NADH oxidase/alkyl hydroperoxide reductase flavoprotein	741
L.B. Poole	The Salmonella typhimurium alkyl hydroperoxide reductase enzyme system	751
H.R. Ellis and L.B. Poole	Characterization of catalytically-important cysteine residues in the AhpC peroxidase protein from Salmonella typhimurium	761
M.L. Calzi and L.B. Poole	Involvement of the two AhpF cystine disulfides in the electron transfer during catalysis of peroxide reduction	765
L.B. Poole, M. Shimada and M. Higuchi	NADH oxidase-1 and a second component encoded upstream of nox1 comprise an alkyl hydroperoxide reductase system in Streptococcus mutans	769
E.J. Crane, III, and A. Claiborne	The role of Arg303 in the structure and mechanism of Enterococcal NADH peroxidase	773
J.I. Yeh, W.G.J. Hol and A. Claiborne	Structure of the native cysteine-sulfenic acid redox center of Enterococcal NADH peroxidase refined at 2.8 Å resolution	777
T.C. Mallett, D. Parsonage and A. Claiborne	NADH oxidase from Enterococcus faecalis: Altered reaction stoichiometry of a C42S mutant	781
D. Toomey, C. Logan, K. Watson and S.G. Mayhew	Properties of NADH oxidase from Thermus aquaticus: Evidence for a function in a peroxide reductase system	785
5. Other
H-Y.M. Cheng and K.J. Stevenson	NAD(P)H oxidase from Thermococcus AN1: Purfication and characterization	791
S. Engst and S.M. Miller	What is the coordination environment of mercuric ion [Hg(II)] in mercuric ion reductase?	795
S. Engst and S.M. Miller	Spectroscopic and thermodynamic characterization of complexes of mercuric ion reductase with pyridine nucleotides	799
L. Kim-Shapiro and S.M. Miller	Synthesis and preliminary characterization of a potential direct probe of asymmetry in mercuric reductase	803
K. Hoober, B. Joneja, H.B. White, III, and C. Thorpe	A sulfhydryl oxidase from chicken egg white	807
Y. Sun, K.A. Costello and K.J. Stevenson	Purification and characterization of NAD(P)H oxidase from Giardia lamblia	811
A.H. Westphal, L. Jacobs, A. de Kok, J. Swaving and J.A.M. de Bont	A new type of disulfide reductase involved in epoxide degradation by Xanthobacter Py2	815
I. Complex Flavoproteins
1. Xanthine Oxidase/Dehydrogenase
R. Hille	The reaction mechanism of xanthine oxidase	821
R.C. Bray, B.D. Howes, R.L. Richards and D.J. Lowe	Evidence that xanthine oxidase does not function by transfer of a terminal oxo-ligand of molybdenum	831
C.H. Harris and V. Massey	The oxidative half-reaction of xanthine dehydrogenase with NAD+ and oxygen	835
K. Okamoto and T. Nishino	A new tight binding inhibitor of xanthine oxidase	839
T. Nishino, Y. Kashima, K. Okamato, T. Iwasaki and T. Nishino	The monomeric form of xanthine dehydrogenase expressed in baculovirus-insect cell system	843
J.T. Rasmussen, L. Berglund and T.E. Petersen	Structural characterization of bovine xanthine oxidoreductase from the milk fat globule membrane	847
Q. Xiang and D.E. Edmondson	Covalent phosphorus incorporation into Comamonas acidovorans xanthine dehydrogenase	851
2. Trimethylamine Dehydrogenase
N.S. Scrutton, E.K. Wilson, M. Mewies and L.C. Packman	Trimethylamine dehydrogenase: Mechanism and assembly of a complex iron-sulfur flavoprotein	857
R.F. Anderson and R. Hille	Electron transfer within trimethylamine dehydrogenase	865
J. Basran, M. Mewies, C-C. Yang, N.S. Scrutton and F.S. Mathews	Molecular recognition of organic ammonium cations by di- and trimethylamine dehydrogenases	869
F.S. Mathews, P. Trickey, J.D. Barton, Z-W. Chen and N. Scrutton	Crystal structures of recombinant wild type and a C30A mutant of trimethylamine dehydrogenase from Methylophilus W3A1	873
3. Other
M.A. Vanoni, E. Verzotti, F. Fischer, M. Coppola, S. Ferretti, G. Zanetti and B. Curti	Glutamate synthase of Azospirillum brasilense	879
D.P. Ballou, G.T. Gassner, D.A. Johnson, H-W. Liu, V. Bandarian, F. Ruzicka and G. Reed	Kinetics of formation of an organic radical in the ascarylose biosynthesis by a protein complex containing FAD, B6 and two [2Fe-2S] centers	889
Y. Lindqvist, G. Lu, G. Schneider and W.H. Campbell	Crystallographic studies of the FAD/NADH binding fragment of corn nitrate reductase	899
G.T. Gassner and D.P. Ballou	Gated electron transfers in the phthalate dioxygenase system	909
F.S. Mathews, Z-W. Chen, T.E. Meyer, M.A. Cusanovich, M. Koh, G. Van Driessche and J.J. Van Beeumen	Structural studies of flavocytochrome c sulfide dehydrogenase from the purple phototropic bacterium Chromatium vinosum	913
F.S. Nielsen and K.F. Jensen	Dihydroorotate dehydrogenase B from Lactococcus lactis consists of subunits encoded by pyrDb and pyrK and contains FMN, FAD and [Fe-S] clusters	917
K. Ratnam, N. Shiraishi, W.H. Campbell and R. Hille	Kinetic studies of the cytochrome c reductase fragment of nitrate reductase	921
P. Rowland, S. Larsen, F.S. Nielsen, O. Bjornberg and K.F. Jensen	Properties of dihydroorotate dehydrogenase A from Lactococcus lactis. Crystallization and three dimensional structure of the enzyme	927
N. Shiraishi and W.H. Campbell	Expression of nitrate reductase FAD-containing fragments in Pichia	931
G. Van den Broeck, F. Verté, L. De Smet, A. Brigé, V. Kostanjevecki, M. Koh, J.J. Van Beeumen, T.E. Meyer, M.A. Cusanovich, Z-W. Chen and F.S. Mathews	Sequence conservation in flavocytochrome c-sulfide dehydrogenase	935
J. Flavoprotein Assembly
E.A. Ceccarelli, J. Ottado, A.R. Krapp and N. Carrillo	Import of a recombinant flavoprotein precursor containing noncovalently bound FAD into isolated chloroplasts	941
D. Jordon, P. Viitanen, Z. Wawrwak, M. Picollelli, K. Bacot, R. Schwartz and J. Thompson	Cloning, overexpression, crystallization, and some kinetic studies on E. coli riboflavin synthase	945
P. Macheroux, S. Austin, T. Jones, R. Dixon and S. Hill	Some properties of NIFL, a regulatory FAD-binding protein from Azotobackter vinelandii	949
K. Sato, Y. Nishina and K. Shiga	Assembling mechanism of FAD, AMP and the two subunits of electron transfer flavoprotein	953
E.K. Wilson, N.S. Scrutton, L. Huang, R. Hille and F.S. Mathews	Electron transfer complex assembly: The association of trimethylamine dehydrogenase with electron transferring flavoprotein	957
List of Participants		961
Author Index		963
Subject Index		967

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