Eckhard Hofmann
Affiliations: | Biophysics | Ruhr University, Bochum |
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Collaborators
Sign in to add collaborator| Nirmalya Chatterjee | collaborator | 2005-2009 | Ruhr University, Bochum |
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Publications
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| Lampret O, Duan J, Hofmann E, et al. (2020) The roles of long-range proton-coupled electron transfer in the directionality and efficiency of [FeFe]-hydrogenases. Proceedings of the National Academy of Sciences of the United States of America |
| Huwald D, Duda S, Gasper R, et al. (2020) Distinctive structural properties of THB11, a pentacoordinate Chlamydomonas reinhardtii truncated hemoglobin with N- and C-terminal extensions. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry |
| Sommerkamp JA, Frankenberg-Dinkel N, Hofmann E. (2019) Crystal structure of the first eukaryotic bilin reductase PEBB reveals a flipped binding mode of dihydrobiliverdin. The Journal of Biological Chemistry |
| Duan J, Mebs S, Laun K, et al. (2019) Geometry of the Catalytic Active Site in [FeFe]-Hydrogenase Is Determined by Hydrogen Bonding and Proton Transfer Acs Catalysis. 2019: 9140-9149 |
| Duan J, Senger M, Esselborn J, et al. (2018) Crystallographic and spectroscopic assignment of the proton transfer pathway in [FeFe]-hydrogenases. Nature Communications. 9: 4726 |
| Vinklárek IS, Bornemann TLV, Lokstein H, et al. (2018) Temperature Dependence of Chlorophyll Triplet Quenching in Two Photosynthetic Light-Harvesting Complexes from Higher Plants and Dinoflagellates. The Journal of Physical Chemistry. B. 122: 8834-8845 |
| Agostini A, Niklas J, Schulte T, et al. (2018) Changing the site energy of per-614 in the Peridinin-chlorophyll a-protein does not alter its capability of chlorophyll triplet quenching. Biochimica Et Biophysica Acta |
| Ledermann B, Schwan M, Sommerkamp JA, et al. (2018) Evolution and molecular mechanism of four-electron reducing ferredoxin-dependent bilin reductases from oceanic phages. The Febs Journal. 285: 339-356 |
| Kertess L, Wittkamp F, Sommer C, et al. (2017) Chalcogenide substitution in the [2Fe] cluster of [FeFe]-hydrogenases conserves high enzymatic activity Dalton Transactions. 46: 16947-16958 |
| Winkler M, Senger M, Duan J, et al. (2017) Accumulating the hydride state in the catalytic cycle of [FeFe]-hydrogenases. Nature Communications. 8: 16115 |