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2020


Stripp, S. T., Mebs, S., Haumann, M.
Temperature Dependence of Structural Dynamics at the Catalytic Cofactor of [FeFe]- hydrogenase
Inorg. Chem. 59 (22): 16474 – 88 (2020); doi.org/10.1021/acs.inorgchem.0c02316


Land, H., Sekretaryova, A. L., Huang, P., Redman, H. J., Németh, B., Polidori, N., Mészáros, L., Senger, M., Stripp, S. T., Berggren, G.
Characterization of a putative sensory [FeFe]-hydrogenase provides new insight into the role of the active site architecture
Chem. Sci. 2020; https://doi.org/10.1039/D0SC03319G


Németh, B., Senger, M., Redman, H. J., Ceccaldi, P., Broderick, J., Magnuson, A., Stripp, S. T., Haumann, M., Berggren, G.
[FeFe]-Hydrogenase Maturation: H-Cluster Assembly Intermediates Tracked by Electron Paramagnetic Resonance, Infrared, and X-Ray Absorption Spectroscopy
J. Biol. Inorg. Chem. 25: 777 – 88 (2020); doi.org/10.1007/s00775-020-01799-8


Land, H., Senger, M., Berggren G., Stripp, S. T.
Current State of [FeFe]-Hydrogenase Research: Biodiversity and Spectroscopic Investigations 
ACS Catal. 10 (13): 7069 – 86 (2020); doi.org/10.1021/acscatal.0c01614


Ulrich, G., P!tzner, E. Hoehl, A. Liao, J-W., Zadvorna, O., Schweicher, G., Sirringhaus, H., Heberle, J., Kästner, B., Wunderlich, J.,  and Venkateshvaran, D.
Thermoelectric nanospectroscopy for the imaging of molecular fingerprints
Nanophotonics 9,  4347–4354 (2020); doi.org/10.1515/nanoph-2020-0316


Janda, T., Godinho, J., Ostatnicky, T., Pfitzner, E.,  Ulrich, G., Hoehl, A., Reimers, S., Šobáˇn, Z., Metzger, T., Reichlová, H., Novák, V.,  Campion, R. P.,  Heberle, J., Wadley, P.,   Edmonds, K. W.,  Amin, O. J., Chauhan, J. S.,   Dhesi, S. S., Maccherozzi, F.,  Otxoa, R. M., Roy, P. E.,  Olejník, K.,  Nˇemec, P.,  Jungwirth, T.,  Kaestner, B., and Wunderlich, J.
Magneto-Seebeck microscopy of domain switching in collinear antiferromagnet CuMnAs
Phys. Rev.  Mat 4, 094413 (2020); doi.org/10.1103/PhysRevMaterials.4.094413


Hugentobler, K. G., Heinrich, D., Berg, J., Heberle, J., Brzezinski, P., Schlesinger, R. and Block, S.
Lipid Composition Affects the Efficiency in the Functional Reconstitution of the Cytochrome c Oxidase
Int. J. Mol. Sci., 21(19), 6981 (2020); doi.org/10.3390/ijms21196981


Pfitzner E, Heberle J.
Infrared Scattering-Type Scanning Near-Field Optical Microscopy of Biomembranes in Water.
J. Phys. Chem. Lett. 11, 8183−8188 (2020), doi: 10.1021/acs.jpclett.0c01769


Skopintsev, P., Ehrenberg, D., Weinert, T., James, D., Kar, R.K., Johnson, P.J.M., Ozerov, D., Furrer, A., Mous, S., Martiel, I., Dworkowski, F., Nass, K., Knopp, G., Cirelli,C., Gashi, D., Wranik, M., Gruhl, T., Kekilli, D., Brünle, S., Deupi, X., Schertler, G., Benoit, R., Panneels, V., Nogly, P., Schapiro, I., Milne,C., Heberle, J., Standfuss, J.
Femtosecond to millisecond structural changes in a light-driven sodium pump
Nature 583, 314–318 (2020), doi: 10.1038/s41586-020-2307-8


Harris A., Lazaratos M., Siemers M., Watt E., Hoang A., Tomida S., Schubert L., Saita M., Heberle J., Furutani Y., Kandori H., Bondar A.N., Brown L.S.
Mechanism of Inward Proton Transport in an Antarctic Microbial Rhodopsin
J Phys Chem B 124 (24), 4851-4872 (2020),  doi: 10.1021/acs.jpcb.0c02767


Mészáros, L.S., Ceccaldi, P., Lorenzi, M., Redman, H.J., Pfitzner, E., Heberle, J., Senger, M., Stripp, S.T., Berggren, G.
Spectroscopic investigations under whole-cell conditions provide new insight into the metal hydride chemistry of [FeFe]-hydrogenase
Chem. Sci. 11, 4608-4617 (2020), doi: 10.1039/D0SC00512F


Kruse F., Nguyen A.D., Dragelj J., Schlesinger R., Heberle J., Mroginski M.A., Weidinger I.M.
Characterisation of the Cyanate Inhibited State of Cytochrome c Oxidase
Sci Rep. Mar 2;10(1):3863 (2020). doi: 10.1038/s41598-020-60801-0.