Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Vera Engelbrecht"'
Autor:
Melanie Heghmanns, Alexander Günzel, Dörte Brandis, Yury Kutin, Vera Engelbrecht, Martin Winkler, Thomas Happe, Müge Kasanmascheff
Publikováno v:
Biophysical Reports, Vol 1, Iss 2, Pp 100016- (2021)
As essential electron translocating proteins in photosynthetic organisms, multiple plant-type ferredoxin (Fdx) isoforms are involved in a high number of reductive metabolic processes in the chloroplast. To allow quick cellular responses under changin
Externí odkaz:
https://doaj.org/article/d529ba1132984672adb7ba49c629a265
Autor:
Jifu Duan, Moritz Senger, Julian Esselborn, Vera Engelbrecht, Florian Wittkamp, Ulf-Peter Apfel, Eckhard Hofmann, Sven T. Stripp, Thomas Happe, Martin Winkler
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
[FeFe]-hydrogenases catalyze H2-evolution and -oxidation at very high turnover-rates. Here the authors provide experimental evidence for the proposed proton-transfer (PT) pathway by kinetically, spectroscopically, and crystallographically characteriz
Externí odkaz:
https://doaj.org/article/4bada01f9d834987b23d9982e7b4807b
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 27:631-640
Abstract Ferredoxins are essential electron transferring proteins in organisms. Twelve plant-type ferredoxins in the green alga Chlamydomonas reinhardtii determine the fate of electrons, generated in multiple metabolic processes. The two hydrogenases
Autor:
Rieke Haas, Vera Engelbrecht, Oliver Lampret, Shanika Yadav, Ulf‐Peter Apfel, Silke Leimkühler, Thomas Happe
Publikováno v:
ChemBioChem.
Autor:
Andreas Rutz, Chandan K. Das, Andrea Fasano, Jan Jaenecke, Shanika Yadav, Ulf-Peter Apfel, Vera Engelbrecht, Vincent Fourmond, Christophe Léger, Lars V. Schäfer, Thomas Happe
Publikováno v:
ACS Catalysis
ACS Catalysis, 2022, 13 (2), pp.856-865. ⟨10.1021/acscatal.2c04031⟩
ACS Catalysis, 2022, 13 (2), pp.856-865. ⟨10.1021/acscatal.2c04031⟩
International audience; The high turnover rates of [FeFe]-hydrogenases under mild conditions and at low overpotentials provide a natural blueprint for the design of hydrogen catalysts. However, the unique active site (H-cluster) degrades upon contact
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5838b67b3b68008ee4155bd7311a46b2
https://hal.science/hal-03932821
https://hal.science/hal-03932821
Autor:
Thomas Happe, Shanika Yadav, Alexander Günzel, Kristina Liedtke, Andreas Rutz, Vera Engelbrecht
Publikováno v:
International Journal of Hydrogen Energy. 46:7165-7175
Gaining knowledge about the algal hydrogen metabolism is prerequisite for the biotechnological exploitation of photosynthetic H2 production. Model organism Chlamydomonas reinhardtii encodes two [FeFe]-hydrogenases, which are individually capable of c
Autor:
Melanie Heghmanns, Andreas Rutz, Yury Kutin, Vera Engelbrecht, Martin Winkler, Thomas Happe, Müge Kasanmascheff
Publikováno v:
Chemical science. 13(24)
[FeFe]-hydrogenases catalyze the reversible conversion of molecular hydrogen into protons and electrons with remarkable efficiency. However, their industrial applications are limited by their oxygen sensitivity. Recently, it was shown that the [FeFe]
Autor:
Melanie Heghmanns, Andreas Rutz, Yury Kutin, Vera Engelbrecht, Martin Winkler, Thomas Happe, Müge Kasanmascheff
Publikováno v:
Chemical Science. 13:8704-8704
Correction for ‘The oxygen-resistant [FeFe]-hydrogenase CbA5H harbors an unknown radical signal’ by Melanie Heghmanns et al., Chem. Sci., 2022, 13, 7289–7294, https://doi.org/10.1039/D2SC00385F.
Autor:
Alexander Günzel, Yury Kutin, Dörte Brandis, Melanie Heghmanns, Vera Engelbrecht, Thomas Happe, Müge Kasanmascheff, Martin Winkler
Publikováno v:
Biophysical Reports. 1:100016
As essential electron translocating proteins in photosynthetic organisms, multiple plant-type ferredoxin (Fdx) isoforms are involved in a high number of reductive metabolic processes in the chloroplast. To allow quick cellular responses under changin
Autor:
Vera, Engelbrecht, Thomas, Happe
Publikováno v:
Methods in enzymology. 613
Algal hydrogenases are among to the most efficient hydrogen (H