Publikationen

Blumenstein, L.; Domratcheva, T.; Niks, D.; Ngo, H.; Seidel, R.; Dunn, M. F.; Schlichting, I.: BetaQ114N and betaT110V mutations reveal a critically important role of the substrate alpha-carboxylate site in the reaction specificity of tryptophan synthase. Biochemistry 46 (49), S. 14100 - 14116 (2007)

Makris, T. M.; von König, K.; Schlichting, I.; Sligar, S. G.: Alteration of P450 distal pocket solvent leads to impaired proton delivery and changes in heme geometry. Biochemistry 46 (49), S. 14129 - 14140 (2007)

Casino, P.; Niks, D.; Ngo, H.; Pan, P.; Brzovic, P.; Blumenstein, L.; Barends, T.; Schlichting, I.; Dunn, M. F.: Allosteric regulation of tryptophan synthase channeling: the internal aldimine probed by trans-3-indole-3'-acrylate binding. Biochemistry 46 (26), S. 7728 - 7739 (2007)

Ngo, H.; Harris, R.; Kimmich, N.; Casino, P.; Niks, D.; Blumenstein, L.; Barends, T.; Kulik, V.; Weyand, M.; Schlichting, I. et al.; Dunn, M. F.: Synthesis and characterization of allosteric probes of substrate channeling in the tryptophan synthase bienzyme complex. Biochemistry 46 (26), S. 7713 - 7727 (2007)

Ngo, H.; Kimmich, N.; Harris, R.; Niks, D.; Blumenstein, L.; Kulik, V.; Barends, T.; Schlichting, I.; Dunn, M. F.: Allosteric regulation of substrate channeling in tryptophan synthase: modulation of the L-serine reaction in stage I of the beta-reaction by alpha-site ligands. Biochemistry 46 (26), S. 7740 - 7753 (2007)

Kühnel, K.; Derat, E.; Terner, J.; Shaik, S.; Schlichting, I.: Structure and quantum chemical characterization of chloroperoxidase compound 0, a common reaction intermediate of diverse heme enzymes. Proceedings of the National Academy of Sciences of the United States of America 104 (1), S. 99 - 104 (2007)

Beitlich, T.; Kühnel, K.; Schulze-Briese, C.; Shoeman, R. L.; Schlichting, I.: Cryoradiolytic reduction of crystalline heme proteins: analysis by UV-Vis spectroscopy and X-ray crystallography. Journal of Synchrotron Radiation 14 (1), S. 11 - 23 (2007)

von König, K.; Schlichting, I.: Cytochromes P450 - structural basis for binding and catalysis. In: Metal ions in life sciences: the ubiquitous roles of cytochrome P450 proteins; Volume 3, Bd. 3, S. 235 - 265 (Hg. Sigel, A.; Sigel, H.; Sigel, R. K. O.). Wiley & Sons Ltd., Chichester, UK (2007)