Single amino acid substitution reveals latent photolyase activity in Arabidopsis cry1

Burney S, Wenzel R, Kottke T, Roussel T, Hoang N, Bouly J-P, Bittl R, Heberle J, Ahmad M (2012)
Angewandte Chemie - International Edition 51(37): 9356-9360.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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DOI
Autor*in
Burney, Sarah; Wenzel, Ringo; Kottke, TilmanUniBi ; Roussel, Thomas; Hoang, Nathalie; Bouly, Jean-Pierre; Bittl, Robert; Heberle, Joachim; Ahmad, Margaret
Einrichtung
Fakultät für Chemie > Physikalische und Biophysikalische Chemie
Stichworte
Oxidation-Reduction; Flavins/chemistry; Arabidopsis/enzymology; Amino Acid Substitution; Arabidopsis Proteins/genetics; Arabidopsis Proteins/metabolism; Cryptochromes/genetics; DNA Repair; Cryptochromes/metabolism; Ultraviolet Rays
Erscheinungsjahr
2012
Zeitschriftentitel
Angewandte Chemie - International Edition
Band
51
Ausgabe
37
Seite(n)
9356-9360
ISSN
1433-7851
Page URI
https://pub.uni-bielefeld.de/record/2561793

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Burney S, Wenzel R, Kottke T, et al. Single amino acid substitution reveals latent photolyase activity in Arabidopsis cry1. Angewandte Chemie - International Edition. 2012;51(37):9356-9360.
Burney, S., Wenzel, R., Kottke, T., Roussel, T., Hoang, N., Bouly, J. - P., Bittl, R., et al. (2012). Single amino acid substitution reveals latent photolyase activity in Arabidopsis cry1. Angewandte Chemie - International Edition, 51(37), 9356-9360. doi:10.1002/anie.201203476
Burney, Sarah, Wenzel, Ringo, Kottke, Tilman, Roussel, Thomas, Hoang, Nathalie, Bouly, Jean-Pierre, Bittl, Robert, Heberle, Joachim, and Ahmad, Margaret. 2012. “Single amino acid substitution reveals latent photolyase activity in Arabidopsis cry1”. Angewandte Chemie - International Edition 51 (37): 9356-9360.
Burney, S., Wenzel, R., Kottke, T., Roussel, T., Hoang, N., Bouly, J. - P., Bittl, R., Heberle, J., and Ahmad, M. (2012). Single amino acid substitution reveals latent photolyase activity in Arabidopsis cry1. Angewandte Chemie - International Edition 51, 9356-9360.
Burney, S., et al., 2012. Single amino acid substitution reveals latent photolyase activity in Arabidopsis cry1. Angewandte Chemie - International Edition, 51(37), p 9356-9360.
S. Burney, et al., “Single amino acid substitution reveals latent photolyase activity in Arabidopsis cry1”, Angewandte Chemie - International Edition, vol. 51, 2012, pp. 9356-9360.
Burney, S., Wenzel, R., Kottke, T., Roussel, T., Hoang, N., Bouly, J.-P., Bittl, R., Heberle, J., Ahmad, M.: Single amino acid substitution reveals latent photolyase activity in Arabidopsis cry1. Angewandte Chemie - International Edition. 51, 9356-9360 (2012).
Burney, Sarah, Wenzel, Ringo, Kottke, Tilman, Roussel, Thomas, Hoang, Nathalie, Bouly, Jean-Pierre, Bittl, Robert, Heberle, Joachim, and Ahmad, Margaret. “Single amino acid substitution reveals latent photolyase activity in Arabidopsis cry1”. Angewandte Chemie - International Edition 51.37 (2012): 9356-9360.

12 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

A Compass at Weak Magnetic Fields Using Thymine Dimer Repair.
Zwang TJ, Tse ECM, Zhong D, Barton JK., ACS Cent Sci 4(3), 2018
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Flavin Adenine Dinucleotide and N5 ,N10 -Methenyltetrahydrofolate are the in planta Cofactors of Arabidopsis thaliana Cryptochrome 3.
Göbel T, Reisbacher S, Batschauer A, Pokorny R., Photochem Photobiol 93(1), 2017
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Residues at a Single Site Differentiate Animal Cryptochromes from Cyclobutane Pyrimidine Dimer Photolyases by Affecting the Proteins' Preferences for Reduced FAD.
Xu L, Wen B, Wang Y, Tian C, Wu M, Zhu G., Chembiochem 18(12), 2017
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Photochemistry of Wild-Type and N378D Mutant E. coli DNA Photolyase with Oxidized FAD Cofactor Studied by Transient Absorption Spectroscopy.
Müller P, Brettel K, Brettel K, Grama L, Nyitrai M, Lukacs A., Chemphyschem 17(9), 2016
PMID: 26852903
Kinetic Modeling of the Arabidopsis Cryptochrome Photocycle: FADH(o) Accumulation Correlates with Biological Activity.
Procopio M, Link J, Engle D, Witczak J, Ritz T, Ahmad M., Front Plant Sci 7(), 2016
PMID: 27446119
Proton transfer to flavin stabilizes the signaling state of the blue light receptor plant cryptochrome.
Hense A, Herman E, Oldemeyer S, Kottke T., J Biol Chem 290(3), 2015
PMID: 25471375
Cellular metabolites modulate in vivo signaling of Arabidopsis cryptochrome-1.
El-Esawi M, Glascoe A, Engle D, Ritz T, Link J, Ahmad M., Plant Signal Behav 10(9), 2015
PMID: 26313597
The class III cyclobutane pyrimidine dimer photolyase structure reveals a new antenna chromophore binding site and alternative photoreduction pathways.
Scheerer P, Zhang F, Kalms J, von Stetten D, Krauß N, Oberpichler I, Lamparter T., J Biol Chem 290(18), 2015
PMID: 25784552
Spectroscopic characterization of radicals and radical pairs in fruit fly cryptochrome - protonated and nonprotonated flavin radical-states.
Paulus B, Bajzath C, Melin F, Heidinger L, Kromm V, Herkersdorf C, Benz U, Mann L, Stehle P, Hellwig P, Weber S, Schleicher E., FEBS J 282(16), 2015
PMID: 25879256
Formation and Direct Repair of UV-induced Dimeric DNA Pyrimidine Lesions.
Kneuttinger AC, Kashiwazaki G, Prill S, Heil K, Müller M, Carell T., Photochem Photobiol 90(1), 2014
PMID: 24354557
Cellular metabolites enhance the light sensitivity of Arabidopsis cryptochrome through alternate electron transfer pathways.
Engelhard C, Wang X, Robles D, Moldt J, Essen LO, Batschauer A, Bittl R, Ahmad M., Plant Cell 26(11), 2014
PMID: 25428980
A radical sense of direction: signalling and mechanism in cryptochrome magnetoreception.
Dodson CA, Hore PJ, Wallace MI., Trends Biochem Sci 38(9), 2013
PMID: 23938034

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