Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Alexander Grundmeier"'
Autor:
Astrid Gräslund, Nina Voevodskaya, Oliver Sanganas, Alexander Grundmeier, Michael Haumann, Friedhelm Lendzian
Publikováno v:
Journal of Biological Chemistry. 284:4555-4566
The R2 protein of class I ribonucleotide reductase (RNR) from Chlamydia trachomatis (Ct) can contain a Mn-Fe instead of the standard Fe-Fe cofactor. Ct R2 has a redox-inert phenylalanine replacing the radical-forming tyrosine of classic RNRs, which i
Publikováno v:
Proceedings of the National Academy of Sciences. 105:17384-17389
The atmospheric dioxygen (O 2 ) is produced at a tetramanganese complex bound to the proteins of photosystem II (PSII). To investigate product inhibition at elevated oxygen partial pressure ( p O 2 ranging from 0.2 to 16 bar), we monitored specifical
Autor:
Holger Dau, Paola Loja, Michael Haumann, Marcos Barra, and Alexander Grundmeier, Roland Krivanek
Publikováno v:
Biochemistry. 45:14523-14532
The Mn4Ca complex bound to photosystem II (PSII) is the active site of photosynthetic water oxidation. Its assembly involves binding and light-driven oxidation of manganese, a process denoted as photoactivation. The disassembly of the Mn complex is a
Autor:
Michael Haumann, Roland Krivanek, Simone Löscher, Paola Loja, Lars-Erik Andreasson, Marcos Barra, Holger Dau, Alexander Grundmeier
Publikováno v:
Biochemistry. 45:13101-13107
Chloride is an important cofactor in photosynthetic water oxidation. It can be replaced by bromide with retention of the oxygen-evolving activity of photosystem II (PSII). Binding of bromide to the Mn(4)Ca complex of PSII in its dark-stable S(1) stat
Autor:
Holger Dau, Alexander Grundmeier
Photosynthetic water oxidation and O2 formation are catalyzed by a Mn4Ca complex bound to the proteins of photosystem II (PSII). The catalytic site, including the inorganic Mn4CaOnHx core and its protein environment, is denoted as oxygen-evolving com
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::182b52878869392072e3c2430e501110
https://doi.org/10.1016/j.bbabio.2011.07.004
https://doi.org/10.1016/j.bbabio.2011.07.004
Autor:
Nina, Voevodskaya, Friedhelm, Lendzian, Oliver, Sanganas, Alexander, Grundmeier, Astrid, Gräslund, Michael, Haumann
Publikováno v:
The Journal of biological chemistry. 284(7)
The R2 protein of class I ribonucleotide reductase (RNR) from Chlamydia trachomatis (Ct) can contain a Mn-Fe instead of the standard Fe-Fe cofactor. Ct R2 has a redox-inert phenylalanine replacing the radical-forming tyrosine of classic RNRs, which i
Publikováno v:
Photosynthesis. Energy from the Sun ISBN: 9781402067075
The water-oxidizing manganese complex bound to the proteins of photosystem II (PSII) was studied by X-ray absorption spectroscopy on PSII membrane particles. An extended range for collection of EXAFS data was used (up to 16.6 A−1). The EXAFS sugges
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::afd7dd0ac71f1679ab9d639c34b46444
https://doi.org/10.1007/978-1-4020-6709-9_91
https://doi.org/10.1007/978-1-4020-6709-9_91
Publikováno v:
Philosophical transactions of the Royal Society of London. Series B, Biological sciences. 363(1494)
The water-oxidizing manganese complex bound to the proteins of photosystem II (PSII) was studied by X-ray absorption spectroscopy on PSII membrane particles. An extended range for collection of extended X-ray absorption fine-structure (EXAFS) data wa
Publikováno v:
Philosophical Transactions of the Royal Society B: Biological Sciences; Mar2008, Vol. 363 Issue 1494, p1237-1244, 8p