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Nitrate reductase molecular biology

Back, E., Dunne, W., Schneiderbauer, A., de Framond, A., Rastogi, R. Rothstein, S.J. (1991). Isolation of the spinach nitrite reductase gene promoter which confers nitrate inducibility on GUS gene expression in transgenic tobacco. Plant Molecular Biology 17, 9-18. [Pg.68]

Choi, H.K., Kleinhofs, A. An, G. (1989). Nucleotide sequence of rice nitrate reductase genes. Plant Molecular Biology 13, 731-3. [Pg.70]

Dorbe, M.-F., Caboche, M. Daniel-Vedele, F. (1992). The tomato NIA gene complements a Nicotiana plumbaginifolia nitrate reductase-deficient mutant and is properly regulated. Plant Molecular Biology 18,.363-75. [Pg.71]

Hyde, G.E., Wilberding, J.A., Meyer, A.L., Campbell, E.R. Campbell, W.H. (1989). Monoclonal antibody-based immunoaffinity chromatography for purifying corn and squash NADH nitrate reductases. Evidence for an interchain disulfide bond in nitrate reductase. Plant Molecular Biology 13, 233-46. [Pg.72]

Lu, J.-L., Ertl, J.R. Chen, C.-M. (1990). Cytokinin enhancement of the light induction of nitrate reductase transcript levels in etiolated barley leaves. Plant Molecular Biology 14, 585-94. [Pg.73]

Prosser, I.M. Lazarus, C.M. (1990). Nucleotide sequence of a spinach nitrate reductase cDNA. Plant Molecular Biology IS, 187-90. [Pg.75]

Solomonson, L.P. Barber, M.J. (1990). Assimilatory nitrate reductase functional properties and regulation. Annual Review of Plant Physiology and Plant Molecular Biology 41, 225-53. [Pg.76]

Vaucheret, H., Kronenberger, J., Rouze, P. Caboche, M. (1989). Complete nucleotide sequence of the two homeologous tobacco nitrate reductase genes. Plant Molecular Biology 12, 597-600. [Pg.76]

An important biological trace element is molybdenum, and it is now well established that it participates in a number of redox reactions, including the oxidation of xanthine and purines and the reduction of nitrate and molecular nitrogen. It seems to be generally accepted that molybdenum is present in the 6+ and 5+ states in the enzymes, probably alternating between the two during active electron transport. Spence has reviewed the biochemical aspects of molybdenum co-ordination chemistry. Kinetic studies have been reported by the same author on a model for nitrate reductase the Mo -catalysed reduction of nitrate by reduced flavin... [Pg.258]

Proton-coupled electron transfer (PCET) is known to play an important role in a variety of biological processes, including microbial iron transport by ferric enterobactin, enzyme catalysis in systems such as fumarate reductase and nitrate reducatase, and dioxygen binding by the non-heme iron protein hemerythrin. " As such, pH-dependent electrochemical studies can play an important role in unraveling these mechanisms. The most heavily studied biological system known to involve PCET is cytochrome c oxidase, the terminal electron-transfer complex of the mitochondrial respiratory chain, which catalyzes the reduction of molecular oxygen to water. ... [Pg.231]

The reduction of nitrate to ammonia is a rather simple chemical process under very complex control in biological systems. In higher plants the assimilation of nitrate involves the acquisition and subsequent reduction of nitrate to ammonia by nitrate and nitrite reductase. Although our understanding of the biochemistry, genetics, and molecular aspects of nitrate assimilation has advanced, a great deal remains to be learned, especially about regulation and... [Pg.113]


See other pages where Nitrate reductase molecular biology is mentioned: [Pg.912]    [Pg.912]    [Pg.296]    [Pg.1437]    [Pg.47]    [Pg.905]    [Pg.3276]    [Pg.89]    [Pg.272]    [Pg.611]    [Pg.834]    [Pg.112]    [Pg.38]    [Pg.834]    [Pg.472]   
See also in sourсe #XX -- [ Pg.97 , Pg.98 ]




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