Universität zu Köln 

Prof. Dr. Günter Schwarz

Institut für Biochemie, Universität zu Köln
email: gschwarz@uni-koeln.de
phone: +49-(0)221 470 6440
website

Running time: 2007 – 2011

Abstract

Assimilatory NAD(P)H:nitrate reductases (NR) catalyse the first step of nitrate assimilation in plants, algae and fungi. Reversible inactivation of plant NR is initiated by phosphorylation of a conserved serine located between the molybdenum domain, where catalysis takes place, and the heme domain followed by binding of a 14-3-3 protein. Our goal is to identify the functional and structural mechanism by which NR activity is turned down via 14-3-3 proteins by using a fully defined in vitro system. We will characterise the biophysical, enzymatic and structural properties of the apo-, the phosphorylated as well as 14-3-3-complexed enzyme.

(A final report will follow.)

Publications resulting from the project:

Lambeck, I., Fischer-Schrader, K., Nick, D., Röper, J., Chi, J.C., Hille, R., Schwarz, G. (2012). The molecular mechanism of 14-3-3-mediated inhibition of plant nitrate reductase.?J. Biol. Chem. 287, 4562-4571.

Mendel, R.R., Schwarz, G. (2011). Molybdenum cofactor biosynthesis in plants and humans.?Coord. Chem. Rev. 255, 1145-58.

Lambeck, I., Chi, J.C., Krizowski, S., Mueller, S., Mehlmer, N., Teige, M., Fischer, K., and Schwarz, G. (2010). Kinetic analysis of 14-3-3-inhibited Arabidopsis thaliana nitrate reductase. Biochemistry 49, 8177-8186.