Mediated electrochemistry of nitrate reductase from Arabidopsis thaliana
作者： Palraj Kalimuthu , Katrin Fischer-Schrader , Günter Schwarz , Paul V. Bernhardt
DOI: 10.1021/JP404076W
关键词:
摘要: Herein we report the mediated electrocatalytic voltammetry of plant molybdoenzyme nitrate reductase (NR) from Arabidopsis thaliana using established truncated molybdenum-heme fragment at a glassy carbon (GC) electrode. Methyl viologen (MV), benzyl (BV), and anthraquinone-2-sulfonic acid (AQ) are employed as effective artificial electron transfer partners for NR, differing in redox potential over range about 220 mV delivering different reductive driving forces to enzyme. Nitrate is reduced Mo active site yielding oxidized form enzyme, which reactivated by electro-reduced mediator. Digital simulation was performed single set enzyme dependent parameters all catalytic obtained under sweep rates various substrate or mediator concentrations. The kinetic constants digital provide new insight into kinetics NR mechanism.
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M G Redinbaugh, W H Campbell, Quaternary structure and composition of squash NADH: nitrate reductase. Journal of Biological Chemistry. ,vol. 260, pp. 3380- 3385 ,(1985) , 10.1016/S0021-9258(19)83632-3
G. Gowri, Wilbur H. Campbell, cDNA Clones for Corn Leaf NADH:Nitrate Reductase and Chloroplast NAD(P):Glyceraldehyde-3-Phosphate Dehydrogenase : Characterization of the Clones and Analysis of the Expression of the Genes in Leaves as Influenced by Nitrate in the Light and Dark. Plant Physiology. ,vol. 90, pp. 792- 798 ,(1989) , 10.1104/PP.90.3.792
Vytas Reipa, S.-M. Laura Yeh, Harold G. Monbouquette, Vincent L. Vilker, Reorientation of Tetradecylmethyl Viologen on Gold upon Coadsorption of Decanethiol and Its Mediation of Electron Transfer to Nitrate Reductase Langmuir. ,vol. 15, pp. 8126- 8132 ,(1999) , 10.1021/LA981371K
Guoguang Lu, Wilbur H Campbell, Gunter Schneider, Ylva Lindqvist, Crystal structure of the FAD-containing fragment of corn nitrate reductase at 2.5å resolution: relationship to other flavoprotein reductases Structure. ,vol. 2, pp. 809- 821 ,(1994) , 10.1016/S0969-2126(94)00082-4
Bettina Frangioni, Pascal Arnoux, Monique Sabaty, David Pignol, Patrick Bertrand, Bruno Guigliarelli, Christophe Léger, In Rhodobacter sphaeroides respiratory nitrate reductase, the kinetics of substrate binding favors intramolecular electron transfer. Journal of the American Chemical Society. ,vol. 126, pp. 1328- 1329 ,(2004) , 10.1021/JA0384072
Catarina Coelho, Jacopo Marangon, David Rodrigues, José J.G. Moura, Maria João Romão, Patrícia M. Paes de Sousa, Margarida M. Correia dos Santos, Induced peroxidase activity of haem containing nitrate reductases revealed by protein film electrochemistry Journal of Electroanalytical Chemistry. ,vol. 693, pp. 105- 113 ,(2013) , 10.1016/J.JELECHEM.2013.01.030
Serge Cosnier, Bruno Galland, Christophe Innocent, New electropolymerizable amphiphilic viologens for the immobilization and electrical wiring of a nitrate reductase Journal of Electroanalytical Chemistry. ,vol. 433, pp. 113- 119 ,(1997) , 10.1016/S0022-0728(97)00207-6
Lawrie Skipper, Wilbur H. Campbell, Jeffrey A. Mertens, David J. Lowe, Pre-steady-state kinetic analysis of recombinant Arabidopsis NADH:nitrate reductase: rate-limiting processes in catalysis Journal of Biological Chemistry. ,vol. 276, pp. 26995- 27002 ,(2001) , 10.1074/JBC.M100356200
Vincent Fourmond, Monique Sabaty, Pascal Arnoux, Patrick Bertrand, David Pignol, Christophe Léger, Reassessing the strategies for trapping catalytic intermediates during nitrate reductase turnover. Journal of Physical Chemistry B. ,vol. 114, pp. 3341- 3347 ,(2010) , 10.1021/JP911443Y
H. Vaucheret, J. Kronenberger, P. Rouz�, M. Caboche, Complete nucleotide sequence of the two homeologous tobacco nitrate reductase genes Plant Molecular Biology. ,vol. 12, pp. 597- 600 ,(1989) , 10.1007/BF00036974