Access the full text.
Sign up today, get DeepDyve free for 14 days.
A. Glatigny, P. Hof, M. Romão, R. Huber, C. Scazzocchio (1998)
Altered specificity mutations define residues essential for substrate positioning in xanthine dehydrogenase.Journal of molecular biology, 278 2
B. Horecker, L. Heppel (1949)
The reduction of cytochrome c by xanthine oxidase.The Journal of biological chemistry, 178 2
S. Sanders, R. Eisenthal, R. Harrison (1997)
NADH oxidase activity of human xanthine oxidoreductase--generation of superoxide anion.European journal of biochemistry, 245 3
V. Massey, D. Edmondson (1970)
On the mechanism of inactivation of xanthine oxidase by cyanide.The Journal of biological chemistry, 245 24
R Perez-Vicente, JM Alamillo, J Cardenas, M Pineda (1992)
Purification and substrate inactivation of xanthine dehydrogenase from Chlamydomonas reinhardtiiBiochem Biophys Acta, 1117
C. Hesberg, R. Hänsch, R. Mendel, F. Bittner (2004)
Tandem Orientation of Duplicated Xanthine Dehydrogenase Genes from Arabidopsis thalianaJournal of Biological Chemistry, 279
John Grant, G. Loake (2000)
Role of reactive oxygen intermediates and cognate redox signaling in disease resistance.Plant physiology, 124 1
CM Harris, V Massey (1997)
The reaction of reduced xanthine dehydrogenase with molecular oxygen. Reaction kinetics and measurement of superoxide radicalJ Biol Chem, 272
E. Triplett, D. Blevins, D. Randall (1980)
Allantoic Acid Synthesis in Soybean Root Nodule Cytosol via Xanthine Dehydrogenase.Plant physiology, 65 6
I. Fridovich (1989)
Superoxide dismutases: an adaptation to a paramagnetic gasJournal of Biological Chemistry, 264
M. Benboubetra, A. Baghiani, D. Atmani, R. Harrison (2004)
Physicochemical and kinetic properties of purified sheep's milk xanthine oxidoreductase.Journal of dairy science, 87 6
Florence Alesandrini, R. Mathis, G. Sype, D. Hérouart, A. Puppo (2003)
Possible roles for a cysteine protease and hydrogen peroxide in soybean nodule development and senescenceNew Phytologist, 158
T. Nishino, T. Nishino (1989)
The nicotinamide adenine dinucleotide-binding site of chicken liver xanthine dehydrogenase. Evidence for alteration of the redox potential of the flavin by NAD binding or modification of the NAD-binding site and isolation of a modified peptide.The Journal of biological chemistry, 264 10
T. Nishino, T. Nishino, L. Schopfer, V. Massey (1989)
The reactivity of chicken liver xanthine dehydrogenase with molecular oxygen.The Journal of biological chemistry, 264 5
Y. Miao, T. Laun, P. Zimmermann, U. Zentgraf (2004)
Targets of the WRKY53 transcription factor and its role during leaf senescence in ArabidopsisPlant Molecular Biology, 55
A. Levine, R. Tenhaken, R. Dixon, C. Lamb (1994)
H2O2 from the oxidative burst orchestrates the plant hypersensitive disease resistance responseCell, 79
V. Massey (1995)
FLAVOPROTEIN STRUCTURE AND MECHANISMThe FASEB Journal, 9
P. Montalbini (1992)
Inhibition of hypersensitive response by allopurinol applied to the host in the incompatible relationship between Phaseolus vulgaris and Uromyces phaseoliJournal of Phytopathology, 134
E. Corte, F. Stirpe (1970)
The regulation of xanthine oxidase. Inhibition by reduced nicotinamide-adenine dinucleotide of rat liver xanthine oxidase type D and of chick liver xanthine dehydrogenase.The Biochemical journal, 117 1
P. Montalbini (2000)
Xanthine dehydrogenase from leaves of leguminous plants: purification, characterization and properties of the enzyme.Journal of Plant Physiology, 156
P. Avis, F. Bergel, R. Bray (1956)
253. Cellular constituents. The chemistry of xanthine oxidase. Part III. Estimations of the co-factors and the catalytic activities of enzyme fractions from cow's milkJournal of The Chemical Society (resumed)
P. Avis, F. Bergel, R. Bray (1955)
Cellular constituents. The chemistry of xanthine oxidase. Part I. The preparation of a crystalline xanthine oxidase from cow's milkJournal of The Chemical Society (resumed)
G. Brychkova, Z. Alikulov, R. Fluhr, M. Sagi (2008)
A critical role for ureides in dark and senescence-induced purine remobilization is unmasked in the Atxdh1 Arabidopsis mutant.The Plant journal : for cell and molecular biology, 54 3
P. Šauer, J. Frébortová, M. Šebela, P. Galuszka, S. Jacobsen, P. Peč, I. Frébort (2002)
Xanthine dehydrogenase of pea seedlings: a member of the plant molybdenum oxidoreductase familyPlant Physiology and Biochemistry, 40
C. Enroth, B. Eger, K. Okamoto, T. Nishino, E. Pai (2000)
Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion.Proceedings of the National Academy of Sciences of the United States of America, 97 20
T. Nishino, K. Okamoto, Y. Kawaguchi, H. Hori, T. Matsumura, B. Eger, E. Pai, T. Nishino (2005)
Mechanism of the Conversion of Xanthine Dehydrogenase to Xanthine OxidaseJournal of Biological Chemistry, 280
E. Garattini, R. Mendel, M. Romão, R. Wright, M. Terao (2003)
Mammalian molybdo-flavoenzymes, an expanding family of proteins: structure, genetics, regulation, function and pathophysiology.The Biochemical journal, 372 Pt 1
T Nishino, K Okamoto, Y Kawaguchi, H Hori, T Matsumura, BT Eger, EF Pai, T Nishino (2005)
Mechanism of the conversion of xanthine dehydrogenase to xanthine oxidase: identification of the two cysteine disulfide bonds and crystal structure of a non-convertible rat liver xanthine dehydrogenase mutantJ Biol Chem, 280
M. Rubio, E. James, María Clemente, B. Bucciarelli, M. Fedorova, C. Vance, M. Becana (2004)
Localization of superoxide dismutases and hydrogen peroxide in legume root nodules.Molecular plant-microbe interactions : MPMI, 17 12
D. Datta, E. Triplett, E. Newcomb (1991)
Localization of xanthine dehydrogenase in cowpea root nodules: implications for the interaction between cellular compartments during ureide biogenesis.Proceedings of the National Academy of Sciences of the United States of America, 88 11
H. Corran, J. Dewan, A. Gordon, D. Green (1939)
Xanthine oxidase and milk flavoprotein: With an Addendum by J. St L. Philpot.The Biochemical journal, 33 10
F. Corpas, M. Gómez, J. Hernández, L. Río (1993)
Metabolism of Activated Oxygen in Peroxisomes from two Pisum sativum L. Cultivars with Different Sensitivity to Sodium ChlorideJournal of Plant Physiology, 141
V. Massey (1959)
The microestimation of succinate and the extinction coefficient of cytochrome c.Biochimica et biophysica acta, 34
Rafael Pérez-Vecinte, J. Alamillo, Jacobo Cárdenas, M. Pineda (1992)
Purification and substrate inactivation of xanthine dehydrogenase from Chlamydomonas reinhardtii.Biochimica et biophysica acta, 1117 2
F. Corpas, J. Palma, L. Sandalio, R. Valderrama, J. Barroso, L. Río (2008)
Peroxisomal xanthine oxidoreductase: characterization of the enzyme from pea (Pisum sativum L.) leaves.Journal of plant physiology, 165 13
V. Massey, P. Brumby, H. Komai (1969)
Studies on milk xanthine oxidase. Some spectral and kinetic properties.The Journal of biological chemistry, 244 7
R. Hille (2006)
Structure and Function of Xanthine OxidoreductaseEuropean Journal of Inorganic Chemistry, 2006
Y. Amaya, K. Yamazaki, M. Sato, K. Noda, T. Nishino (1990)
Proteolytic conversion of xanthine dehydrogenase from the NAD-dependent type to the O2-dependent type. Amino acid sequence of rat liver xanthine dehydrogenase and identification of the cleavage sites of the enzyme protein during irreversible conversion by trypsin.The Journal of biological chemistry, 265 24
P. Evans, D. Gallesi, C. Mathieu, María Hernández, M. Felipe, B. Halliwell, A. Puppo (1999)
Oxidative stress occurs during soybean nodule senescencePlanta, 208
A Sato, T Nishino, K Noda, Y Amaya, T Nishino (1995)
The structure of chicken liver xanthine dehydrogenase. cDNA cloning and the domain structureJ Biol Chem, 270
F. Corpas, Clara Colina, Francisco Sánchez-Rasero, L. Río (1997)
A role for leaf peroxisomes in the catabolism of purinesJournal of Plant Physiology, 151
R Hille, T Nishino (1995)
Flavoprotein structure and mechanism. 4. Xanthine oxidase and xanthine dehydrogenaseFASEB J, 9
Zhazira Yesbergenova, Guohua Yang, E. Oron, D. Soffer, R. Fluhr, M. Sagi (2005)
The plant Mo-hydroxylases aldehyde oxidase and xanthine dehydrogenase have distinct reactive oxygen species signatures and are induced by drought and abscisic acid.The Plant journal : for cell and molecular biology, 42 6
C Hesberg, R Haensch, RR Mendel, F Bittner (2004)
Tandem orientation of duplicated xanthine dehydrogenase genes from Arabidopsis thaliana: differential gene expression and enzyme activitiesJ Biol Chem, 279
Y. Kuwabara, T. Nishino, K. Okamoto, T. Matsumura, B. Eger, E. Pai, T. Nishino (2003)
Unique amino acids cluster for switching from the dehydrogenase to oxidase form of xanthine oxidoreductaseProceedings of the National Academy of Sciences of the United States of America, 100
C. Harris, V. Massey (1997)
The Reaction of Reduced Xanthine Dehydrogenase with Molecular OxygenThe Journal of Biological Chemistry, 272
R. Harrison (2002)
Structure and function of xanthine oxidoreductase: where are we now?Free radical biology & medicine, 33 6
E. Corte, G. Gozzetti, F. Novello, F. Stirpe (1969)
Properties of the xanthine oxidase from human liver.Biochimica et biophysica acta, 191 1
Renata Santos, D. Hérouart, S. Sigaud, D. Touati, A. Puppo (2001)
Oxidative burst in alfalfa-Sinorhizobium meliloti symbiotic interaction.Molecular plant-microbe interactions : MPMI, 14 1
R. Hille, T. Nishino (1995)
Xanthine oxidase and xanthine dehydrogenaseThe FASEB Journal, 9
P. Montalbini (1998)
Purification and some properties of xanthine dehydrogenase from wheat leavesPlant Science, 134
V. Massey, H. Komai, G. Palmer, G. Elion (1970)
On the mechanism of inactivation of xanthine oxidase by allopurinol and other pyrazolo[3,4-d]pyrimidines.The Journal of biological chemistry, 245 11
K. Rajagopalan, P. Handler (1967)
Purification and properties of chicken liver xanthine dehydrogenase.The Journal of biological chemistry, 242 18
M. Bradford (1976)
A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.Analytical biochemistry, 72
Russ HilleS, Vincent Massey (1981)
Studies on the oxidative half-reaction of xanthine oxidase.The Journal of biological chemistry, 256 17
T. Nishino, T. Nishino (1997)
The Conversion from the Dehydrogenase Type to the Oxidase Type of Rat Liver Xanthine Dehydrogenase by Modification of Cysteine Residues with Fluorodinitrobenzene*The Journal of Biological Chemistry, 272
C. Lamb, R. Dixon (1997)
THE OXIDATIVE BURST IN PLANT DISEASE RESISTANCE.Annual review of plant physiology and plant molecular biology, 48
G. Pastori, L. Río (1997)
Natural Senescence of Pea Leaves (An Activated Oxygen-Mediated Function for Peroxisomes), 113
MJ Boland (1981)
NAD+: xanthine dehydrogenase from nodules of navy beans: partial purification and propertiesBiochem Int, 2
F. Stirpe, M. Ravaioli, M. Battelli, S. Musiani, G. Grazi (2002)
Xanthine oxidoreductase activity in human liver diseaseAmerican Journal of Gastroenterology, 97
P. Escuredo, F. Minchin, Y. Gogorcena, I. Iturbe-Ormaetxe, R. Klucas, M. Becana (1996)
Involvement of Activated Oxygen in Nitrate-Induced Senescence of Pea Root Nodules, 110
P. Montalbini (1992)
Ureides and enzymes of ureide synthesis in wheat seeds and leaves and effect of allopurinol on Puccinia recondita f. sp. tritici infectionPlant Science, 87
A. Sato, T. Nishino, K. Noda, Y. Amaya, T. Nishino (1995)
The Structure of Chicken Liver Xanthine DehydrogenaseThe Journal of Biological Chemistry, 270
E. Landon, M. Myles (1967)
NADH oxidation by hypoxanthine dehydrogenase of avian kidney.Biochimica et biophysica acta, 143 2
Xanthine dehydrogenase AtXDH1 from Arabidopsis thaliana is a key enzyme in purine degradation where it oxidizes hypoxanthine to xanthine and xanthine to uric acid. Electrons released from these substrates are either transferred to NAD+ or to molecular oxygen, thereby yielding NADH or superoxide, respectively. By an alternative activity, AtXDH1 is capable of oxidizing NADH with concomitant formation of NAD+ and superoxide. Here we demonstrate that in comparison to the specific activity with xanthine as substrate, the specific activity of recombinant AtXDH1 with NADH as substrate is about 15-times higher accompanied by a doubling in superoxide production. The observation that NAD+ inhibits NADH oxidase activity of AtXDH1 while NADH suppresses NAD+-dependent xanthine oxidation indicates that both NAD+ and NADH compete for the same binding-site and that both sub-activities are not expressed at the same time. Rather, each sub-activity is determined by specific conditions such as the availability of substrates and co-substrates, which allows regulation of superoxide production by AtXDH1. Since AtXDH1 exhibits the most pronounced NADH oxidase activity among all xanthine dehydrogenase proteins studied thus far, our results imply that in particular by its NADH oxidase activity AtXDH1 is an efficient producer of superoxide also in vivo.
Plant Molecular Biology – Springer Journals
Published: Nov 14, 2009
Read and print from thousands of top scholarly journals.
Already have an account? Log in
Bookmark this article. You can see your Bookmarks on your DeepDyve Library.
To save an article, log in first, or sign up for a DeepDyve account if you don’t already have one.
Copy and paste the desired citation format or use the link below to download a file formatted for EndNote
Access the full text.
Sign up today, get DeepDyve free for 14 days.
All DeepDyve websites use cookies to improve your online experience. They were placed on your computer when you launched this website. You can change your cookie settings through your browser.