Publikationen Hartmut Michel

Zeitschriftenartikel (6)

2021
Zeitschriftenartikel
Grund, T. N.; Radloff, M.; Wu, D.; Goojani, H. G.; Witte, L. F.; Jösting, W.; Buschmann, S.; Müller, H.; Elamri, I.; Welsch, S. et al.; Schwalbe, H.; Michel, H.; Bald, D.; Safarian, S.: Mechanistic and structural diversity between cytochrome bd isoforms of Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America 118 (50), e2114013118 (2021)
Zeitschriftenartikel
Kolbe, F.; Safarian, S.; Piórek, Ż.; Welsch, S.; Müller, H.; Michel, H.: Cryo-EM structures of intermediates suggest an alternative catalytic reaction cycle for cytochrome c oxidase. Nature Communications 12, 6903 (2021)
Zeitschriftenartikel
Zhao, J.; Xie, H.; Mehdipour, A. R.; Safarian, S.; Ermler, U.; Münke, C.; Thielmann, Y.; Hummer, G.; Ebersberger, I.; Wang, J. et al.; Michel, H.: The structure of the Aquifex aeolicus MATE family multidrug resistance transporter and sequence comparisons suggest the existence of a new subfamily. Proceedings of the National Academy of Sciences of the United States of America 118 (46), e2107335118 (2021)
Zeitschriftenartikel
Safarian, S.; Opel-Reading, H. K.; Wu, D.; Mehdipour, A. R.; Hards, K.; Harold, L. H.; Radloff, M.; Stewart, I.; Welsch, S.; Hummer, G. et al.; Cook, G. M.; Krause, K. L.; Michel, H.: The cryo-EM structure of the bd oxidase from M. tuberculosis reveals a unique structural framework and enables rational drug design to combat TB. Nature Communications 12 (1), 5236 (2021)
Zeitschriftenartikel
Nikolaev, A.; Safarian, S.; Thesseling, A.; Wohlwend, D.; Friedrich, T.; Michel, H.; Kusumoto, T.; Sakamoto, J.; Melin, F.; Hellwig, P.: Electrocatalytic evidence of the diversity of the oxygen reaction in the bacterial bd oxidase from different organisms. Biochimica et Biophysica Acta, Bioenergetics 1862 (8), e148436 (2021)
Zeitschriftenartikel
Zhu, G.; Zeng, H.; Zhang, S.; Juli, J.; Tai, L.; Zhang, D.; Pang , X.; Zhang, Y.; Lam, S. M.; Zhu, Y. et al.; Peng, G.; Michel, H.; Sun, F.: The unusual homodimer of a heme‐copper terminal oxidase allows itself to utilize two electron donors. Angewandte Chemie, International Edition in English 60 (24), S. 13323 - 13330 (2021)
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