Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Kajsa G. V. Havelius"'
Autor:
Michael Haumann, Nina Voevodskaya, Astrid Gräslund, Kajsa G. V. Havelius, Ana Popović-Bijelić, Petko Chernev, Nils Leidel
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1817(3):430-444
Ribonucleotide reductases (RNRs) are essential for DNA synthesis in most organisms. In class-Ic RNR from Chlamydia trachomatis (Ct), a MnFe cofactor in subunit R2 forms the site required for enzyme activity, instead of an FeFe cofactor plus a redox-a
Publikováno v:
Biochemistry. 51:2054-2064
Cryogenic illumination of Photosystem II (PSII) can lead to the trapping of the metastable radical Y(Z)(•), the radical form of the redox-active tyrosine residue D1-Tyr161 (known as Y(Z)). Magnetic interaction between this radical and the CaMn(4) c
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1807(1):11-21
Metalloradical EPR signals have been found in intact Photosystem II at cryogenic temperatures. They reflect the light-driven formation of the tyrosine Z radical (Y(Z)) in magnetic interaction with the CaMn(4) cluster in a particular S state. These so
Publikováno v:
Applied Magnetic Resonance. 37:151-176
The redox-active tyrosine residue (Y-Z) plays a crucial role in the mechanism of the water oxidation. Metalloradical electron paramagnetic resonance (EPR) signals reflecting the light-induced Y-Z c ...
Publikováno v:
Biochemistry. 48:9393-9404
Water oxidation in photosystem II is catalyzed by the CaMn(4) cluster. The electrons extracted from the CaMn(4) cluster are transferred to P(680)(+) via the redox-active tyrosine residue D1-Tyr161 (Y(Z)). The oxidation of Y(Z) is coupled to a deproto
Publikováno v:
Biochemistry. 46:7865-7874
The photosystem II (PSII) reaction center contains two redox active tyrosines, YZ and YD, situated on the D1 and D2 proteins, respectively. By illumination at 5 K, oxidation of YZ in oxygen-evolving PSII can be observed as induction of the Split S1 E
Autor:
Petko Chernev, Michael Haumann, Sascha Ott, Kajsa G. V. Havelius, Lennart Schwartz, Nils Leidel
Publikováno v:
Journal of the American Chemical Society. 134(34)
High-resolution X-ray absorption spectroscopy with narrow-band X-ray emission detection, supported by density functional theory calculations (XAES-DFT), was used to study a model complex, ([Fe(2)(μ-adt)(CO)(4)(PMe(3))(2)] (1, adt = S-CH(2)-(NCH(2)Ph
Publikováno v:
Inorganic chemistry. 51(8)
The active site for hydrogen production in [FeFe] hydrogenase comprises a diiron unit. Bioinorganic chemistry has modeled important features of this center, aiming at mechanistic understanding and the development of novel catalysts. However, new assa
Autor:
Thomas Happe, Martin Winkler, Jens Noth, Nils Leidel, Camilla Lambertz, Petko Chernev, Michael Haumann, Kajsa G. V. Havelius
Publikováno v:
The Journal of biological chemistry. 286(47)
Irreversible inhibition by molecular oxygen (O(2)) complicates the use of [FeFe]-hydrogenases (HydA) for biotechnological hydrogen (H(2)) production. Modification by O(2) of the active site six-iron complex denoted as the H-cluster ([4Fe4S]-2Fe(H)) o
Autor:
Carola Schulzke, Alexander Döring, Prinson P. Samuel, Silke Leimkühler, Kajsa G. V. Havelius, Sebastian Horn, Stefan Reschke, Michael Haumann
Ten square-based pyramidal molybdenum complexes with different sulfur donor ligands, that is, a variety of dithiolenes and sulfides, were prepared, which mimic coordination motifs of the molybdenum cofactors of molybdenum-dependent oxidoreductases. T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a16bd6874446b6940f4283d57c3b4db
https://publishup.uni-potsdam.de/frontdoor/index/index/docId/36567
https://publishup.uni-potsdam.de/frontdoor/index/index/docId/36567