Springe direkt zu Inhalt

2019

Huang, G., Wagner, T., Wodrich, M.D., Ataka, K., Bill, E., Ermler, U., Hu, X., Shima, S.
The atomic-resolution crystal structure of activated [Fe]-hydrogenase
Nature Catalysis 2, 537-543 (2019)


Ehrenberg, D., Krause, N., Saita, M., Bamann, C., Kar, R.K., Hoffmann, K.,  Heinrich, D., Schapiro, I., Heberle, J., and Schlesinger, R.
Atomistic insight into the role of threonine 127 in the functional mechanism of channelrhodopsin-2
Appl. Sci. 2019, 9(22), 4905; https://doi.org/10.3390/app9224905


Kopyshev, A., Kanevche, K., Lomadze, N., Pfitzner, E., Loebner, S., Patil, R.R., Genzer, J., Heberle, J., Santer, S.
Light-Induced Structuring of Photosensitive Polymer Brushes
ACS Appl. Polym. Mater. 2019, 1, 11, 3017-3026


Senger, M., Eichmann, V., Laun, K., Duan, J., Wittkamp, F., Knör, G., Apfel, U.-P., Happe, T., Winkler, M., Heberle, J., Stripp, S. T.
How [FeFe]-Hydrogenase Facilitates Bidirectional Proton Transfer
J. Am. Chem. Soc. (2019), doi.org/10.1021/jacs.9b09225


Land, H., Ceccaldi, P., Mészáros, L. S., Lorenzi, M.,  Redman, H. J., Senger, M., Stripp, S. T., Berggren, G.,
Discovery of novel [FeFe]-hydrogenases for biocatalytic H2-production
Chem. Sci., (2019), Advance Article, doi 10.1039/C9SC03717A


Duan, J., Mebs, S., Laun, K., Wittkamp, F., Heberle, J., Happe, T., Hofmann, E., Apfel, U.-P., Winkler, M., Senger, M., Haumann, M., Stripp, S.T.
Geometry of the Catalytic Active Site in [FeFe]-Hydrogenase Is Determined by Hydrogen Bonding and Proton Transfer
ACS Catal. (2019), 9, 10, 9140-9149. doi.org/10.1021/acscatal.9b02203

Nass Kovacs, G., Colletier, J.-P. , Grünbein, M. L., Yang, Y., Stensitzki, T. , Batyuk, A., Carbajo, S., Doak, R. B., Ehrenberg, D., Foucar, L., Gasper, R., Gorel, A.,  Hilpert, M., Kloos, M., Koglin, J. E., Reinstein, J., Roome, C. M., Schlesinger, R., Seaberg, M., Shoeman, R. L.,  Stricker, M., Boutet, S., Haacke, S.,  Heberle, J., Heyne, K., Domratcheva, T., Barends, T. R. M., and Schlichting, I.
Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin
Nat. Commun. 10(1): 3177 (2019). doi 10.1038/s41467-019-10758-0


Pan, H.J., Huang, G., Wodrich, M.D., Tirani, F.F., Ataka, K., Shima, S., Hu, X.
A catalytically active [Mn]-hydrogenase incorporating a non-native metal cofactor
Nat Chem. (2019) Jul;11(7):669-675. doi: 10.1038/s41557-019-0266-1


Watanabe, T.,  Wagner, T.,  Huang, G.,  Kahnt, J., Ataka, K., Ermler, U., Shima, S.
The Bacterial [Fe]-Hydrogenase Paralog HmdII Uses Tetrahydrofolate Derivatives as Substrates
Angew. Chem. 58, 3506-3510 (2019), doi: https://doi.org/10.1002/anie.201813465


Mebs, S., Duan, J., Wittkamp, F., Stripp, S. T., Happe, T., Apfel, U.-P., Winkler, M., and Haumann, M.
Differential Protonation at the Catalytic Six-Iron Cofactor of [FeFe]-Hydrogenases Revealed by 57Fe Nuclear Resonance X-ray Scattering and Quantum Mechanics/Molecular Mechanics Analyses

Inorg. Chem. (2019), DOI: 10.1021/acs.inorgchem.9b00100


Ehrenberg, D., Varma, N., Deupi, X., Koyanagi, M., Terakita, A., Schertler, G.F.X., Heberle, J., Lesca, E.
The two-photon reversible reaction of the bistable jumping spider rhodopsin-1
Biophysical Journal 116, 1248–1258 (2019), doi: https://doi.org/10.1016/j.bpj.2019.02.025