Solid-state NMR studies of cofactor-protein systems with functional hydrogen bonds
Zusammenfassung der Projektergebnisse
The main results of this project can be summarized as follows. (1) Novel insights into the properties of active sites of proteins can be obtained by combining studies of specifically labeled protein side chains with studies of active site model compounds and environments, in particular aprotic polar solvents and polypeptides. (2) Acid-base hydrogen bonds behave in the interior of proteins in a similar way as in aprotic polar solvents. (3) 15N chemical shifts of heterocylic nitrogen as in histidines and in lysine side chains can be used to derive estimates of hydrogen bond geometries. (4) models of the structure of transient reaction intermediates of super-oxide dismutates were developed. (5) 51V-solid state NMR techniques for the investigation of vanadium containing enzymes were developed.
Projektbezogene Publikationen (Auswahl)
- Coupling of Functional Hydrogen Bonds in Pyridoxal-5’-phosphate-Enzyme Model Systems Observed by Solid State NMR Spectroscopy J. Am. Chem. Soc. 2007, 129, 4440-4455
S. Sharif, D. Schagen, M. D. Toney, H. H. Limbach
(Siehe online unter https://dx.doi.org/10.1021/ja066240h) - NMR Studies of Coupled Low- and High-Barrier Hydrogen Bonds in Pyridoxal-5’- phosphate Model Systems in Polar Solution. J. Am. Chem. Soc. 2007, 129, 6313-6327
S. Sharif, G. S. Denisov, M. D. Toney, H. H. Limbach
(Siehe online unter https://dx.doi.org/10.1021/ja070296+) - Effects of Hydration on the Acid-Base Interactions and Secondary Structures of Poly-L- Lysine Probed by 15N and 13C Solid State NMR Phys. Chem. Chem. Phys., 2010, 12, 10235-10245
A. Dos, V. Schimming, M. Chan-Huot, H. H. Limbach
(Siehe online unter https://dx.doi.org/10.1039/C002730H) - NMR studies of the Stability, Protonation States and Tautomerism of 13C and 15N Labeled Aldimines of the Coenzyme Pyridoxal 5’-phosphate in Water Biochemistry, 2010, 49, 10818-10830
M. Chan-Huot, S. Sharif, P. M. Tolstoy, M. D. Toney, H. H. Limbach
(Siehe online unter https://dx.doi.org/10.1021/bi101061m) - A Simple Method for Analyzing 51V-Solid State NMR Spectra of Complex Systems Solid State NMR 2011, 40, 60-65
A. Fenn, M. Wächtler, H. Breitzke, A. Buchholz, W. Plass, G. Buntkowsky
(Siehe online unter https://dx.doi.org/10.1016%2Fj.ssnmr.2011.05.001) - Revealing the position of the substrate in NiSOD: a model study. Ang. Chem. Int.Ed., 2011, 50, 2946-2950
D. Tietze, S. Voigt, D. Mollenhauer, M. Tischler, D. Imhof, T. Gutmann, L. González, O. Ohlenschläger, H. Breitzke, M. Görlach, G. Buntkowsky
(Siehe online unter https://doi.org/10.1002/anie.201005027) - NMR Studies of Protonation and Hydrogen Bond States of Internal Aldimines of Pyridoxal 5'-Phosphate Acid-Base in Alanine Racemase, Aspartate Aminotransferase and Poly-L- Lysine J. Am. Chem. Soc. 2013, 135
M. Chan-Huot, A. Dos, R. Zander, S. Sharif, P. M. Tolstoy, S. Compton, E. Fogle, M. D. Toney, I. G. Shenderovich, G. S. Denisov, H. H. Limbach
(Siehe online unter https://doi.org/10.1021/ja408988z) - NMR Studies of Active-Site Properties of Human Carbonic Anhydrase II by using 15N-labeled 4-Methylimidazole as a local Probe and Histidine Hydrogen-Bond Correlations. Chemistry . Volume21, Issue7, February 9, 2015, Pages 2915-2929
I. G. Shenderovich, S. B. Lesnichin, Ch. Tu, D. N. Silverman, P. M. Tolstoy, G. S. Denisov, H. H. Limbach
(Siehe online unter https://doi.org/10.1002/chem.201404083)
