Seminar Bioanorganische Chemie

Vorschläge für Seminarvorträge:

1. VERGEBEN Bandyopadhyay, S.; Chaudhury, S.; Mehta, D.; Ramesh, A., Discovery of iron-sensing bacterial riboswitches. Nature Chemical Biology 2020. Doi: 10.1038/s41589-020-00665-7  (zurückgezogener Artikel)
2. VERGEBEN Brown, B. N.; Robinson, K. J.; Durfee, Q. C.; Kekilli, D.; Hough, M. A.; Andrew, C. R., Hydroxylamine Complexes of Cytochrome c′: Influence of Heme Iron Redox State on Kinetic and Spectroscopic Properties. Inorg. Chem. 2020, 59 (19), 14162-14170. Doi: 10.1021/acs.inorgchem.0c01925
3. Chongdar, N.; Pawlak, K.; Rüdiger, O.; Reijerse, E. J.; Rodríguez-Maciá, P.; Lubitz, W.; Birrell, J. A.; Ogata, H., Spectroscopic and biochemical insight into an electron-bifurcating [FeFe] hydrogenase. J. Biol. Inorg. Chem. 2020, 25 (1), 135-149. Doi: 10.1007/s00775-019-01747-1
4. VERGEBEN Coleman, T.; Stok, J. E.; Podgorski, M. N.; Bruning, J. B.; De Voss, J. J.; Bell, S. G., Structural insights into the role of the acid-alcohol pair of residues required for dioxygen activation in cytochrome P450 enzymes. J. Biol. Inorg. Chem. 2020, 25 (4), 583-596. Doi: 10.1007/s00775-020-01781-4
5. VERGEBEN Cristaldi, J. C.; Ferroni, F. M.; Duré, A. B.; Ramírez, C. S.; Dalosto, S. D.; Rizzi, A. C.; González, P. J.; Rivas, M. G.; Brondino, C. D., Heterologous production and functional characterization of Bradyrhizobium japonicum copper-containing nitrite reductase and its physiological redox partner cytochrome c550. Metallomics 2020, 12 (12), 2084-2097. Doi: 10.1039/D0MT00177E
6. VERGEBEN Harris, D. F.; Jimenez-Vicente, E.; Yang, Z.-Y.; Hoffman, B. M.; Dean, D. R.; Seefeldt, L. C., CO as a substrate and inhibitor of H+ reduction for the Mo-, V-, and Fe-nitrogenase isozymes. J. Inorg. Biochem. 2020, 213, 111278. Doi: https://doi.org/10.1016/j.jinorgbio.2020.111278
7. VERGEBEN Huwald, D.; Duda, S.; Gasper, R.; Olieric, V.; Hofmann, E.; Hemschemeier, A., Distinctive structural properties of THB11, a pentacoordinate Chlamydomonas reinhardtii truncated hemoglobin with N- and C-terminal extensions. J. Biol. Inorg. Chem. 2020, 25 (2), 267-283. Doi: 10.1007/s00775-020-01759-2
8. VERGEBEN Koebke, K. J.; Alfaro, V. S.; Pinter, T. B. J.; Deb, A.; Lehnert, N.; Tard, C.; Penner-Hahn, J. E.; Pecoraro, V. L., Traversing the Red–Green–Blue Color Spectrum in Rationally Designed Cupredoxins. J. Am. Chem. Soc. 2020, 142 (36), 15282-15294. Doi: 10.1021/jacs.0c04757
9. VERGEBEN Li, J.; Davis, I.; Griffith, W. P.; Liu, A., Formation of Monofluorinated Radical Cofactor in Galactose Oxidase through Copper-Mediated C–F Bond Scission. J. Am. Chem. Soc. 2020, 142 (44), 18753-18757. Doi: 10.1021/jacs.0c08992
10. VERGEBEN Louka, S.; Barry, S. M.; Heyes, D. J.; Mubarak, M. Q. E.; Ali, H. S.; Alkhalaf, L. M.; Munro, A. W.; Scrutton, N. S.; Challis, G. L.; de Visser, S. P., Catalytic Mechanism of Aromatic Nitration by Cytochrome P450 TxtE: Involvement of a Ferric-Peroxynitrite Intermediate. J. Am. Chem. Soc. 2020, 142 (37), 15764-15779. Doi: 10.1021/jacs.0c05070
11. VERGEBEN Mahor, D.; Püschmann, J.; van den Haak, M.; Kooij, P. J.; van den Ouden, D. L. J.; Strampraad, M. J. F.; Srour, B.; Hagedoorn, P.-L., A traffic light enzyme: acetate binding reversibly switches chlorite dismutase from a red- to a green-colored heme protein. J. Biol. Inorg. Chem. 2020, 25 (4), 609-620. Doi: 10.1007/s00775-020-01784-1
12. VERGEBEN Musiani, F.; Broll, V.; Evangelisti, E.; Ciurli, S., The model structure of the copper-dependent ammonia monooxygenase. J. Biol. Inorg. Chem. 2020, 25 (7), 995-1007. Doi: 10.1007/s00775-020-01820-0
13. VERGEBEN 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. 2020, 25 (5), 777-788. Doi: doi.org/10.1007/s00775-020-01799-8
14. Rizzolo, K.; Weitz, A. C.; Cohen, S. E.; Drennan, C. L.; Hendrich, M. P.; Elliott, S. J., A Stable Ferryl Porphyrin at the Active Site of Y463M BthA. J. Am. Chem. Soc. 2020, 142 (28), 11978-11982. Doi: https://doi.org/10.1021/jacs.0c04023
15. VERGEBEN Terán, A.; Jaafar, A.; Sánchez-Peláez, A. E.; Torralba, M. C.; Gutiérrez, Á., Design and catalytic studies of structural and functional models of the catechol oxidase enzyme. J. Biol. Inorg. Chem. 2020, 25 (4), 671-683. Doi: 10.1007/s00775-020-01791-2
16. VERGEBEN Tian, S.; Jones, S. M.; Solomon, E. I., Role of a Tyrosine Radical in Human Ceruloplasmin Catalysis. ACS Central Science 2020, 6 (10), 1835-1843. Doi: https://doi.org/10.1021/acscentsci.0c00953
17. VERGEBEN Uhlemann, E.-M. E.; Yu, C. H.; Patry, J.; Dolgova, N.; Lutsenko, S.; Muyldermans, S.; Dmitriev, O. Y., Nanobodies against the metal binding domains of ATP7B as tools to study copper transport in the cell. Metallomics 2020, 12 (12), 1941-1950. Doi: http://dx.doi.org/10.1039/D0MT00191K
18. Weitz, A. C.; Biswas, S.; Rizzolo, K.; Elliott, S.; Bominaar, E. L.; Hendrich, M. P., Electronic State of the His/Tyr-Ligated Heme of BthA by Mössbauer and DFT Analysis. Inorg. Chem. 2020, 59 (14), 10223-10233. Doi: https://doi.org/10.1021/acs.inorgchem.0c01349
19. VERGEBEN Wilson, M.; Tillery, L.; Tabaie, E.; Beery, G.; Preusker, J.; Bhola, I.; Frato, K., Alanine to serine substitutions drive thermal adaptation in a psychrophilic diatom cytochrome c6. J. Biol. Inorg. Chem. 2020, 25 (3), 489-500. Doi: https://doi.org/10.1007/s00775-020-01777-0
20. Zhou, X.; Zhang, X.-P.; Li, W.; Phillips, D. L.; Ke, Z.; Zhao, C., Electronic Effect on Bimetallic Catalysts: Cleavage of Phosphodiester Mediated by Fe(III)–Zn(II) Purple Acid Phosphatase Mimics. Inorg. Chem. 2020, 59 (17), 12065-12074. Doi: https://doi.org/10.1021/acs.inorgchem.0c01011