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of 78
pro vyhledávání: '"Lena J, Daumann"'
Autor:
Lena J. Daumann
Publikováno v:
ACS Central Science, Vol 7, Iss 11, Pp 1780-1782 (2021)
Externí odkaz:
https://doaj.org/article/07c6bd542d924a0bb5ac145a7d0b8cc1
Autor:
Rob A. Schmitz, Nunzia Picone, Helena Singer, Andreas Dietl, Kerstin-Anikó Seifert, Arjan Pol, Mike S. M. Jetten, Thomas R. M. Barends, Lena J. Daumann, Huub J. M. Op den Camp
Publikováno v:
mBio, Vol 12, Iss 5 (2021)
Lanthanides comprise a group of 15 elements with atomic numbers 57 to 71 that are essential in a variety of high-tech devices, such as mobile phones, but were considered biologically inert for a long time. The biological relevance of lanthanides beca
Externí odkaz:
https://doaj.org/article/1286e4c991f3464180b185464a40a2f1
Publikováno v:
Synthesis. 55:1000-1006
Pyrroloquinoline quinone (PQQ) is an important cofactor of methanol dehydrogenases and glycose dehydrogenases. In addition, isolated PQQ is used as a central component in sensors and biomimetic complexes. The synthesis of PQQ derivatives is of intere
Publikováno v:
Angewandte Chemie (International Ed. in English)
The epigenetic marker 5‐methyl‐2′‐deoxycytidine (5mdC) is the most prevalent modification to DNA. It is removed inter alia via an active demethylation pathway: oxidation by Ten‐Eleven Translocation 5‐methyl cytosine dioxygenase (TET) and
Autor:
Henning Lumpe, Violeta A. Vetsova, Alexander Schäfer, Patrick Weis, Lena J. Daumann, Katherine R. Fisher, Erik K. Schneider
Publikováno v:
Chemistry (Weinheim an Der Bergstrasse, Germany)
Chemistry-A European Journal, 27 (39), 10087-10098
Chemistry-A European Journal, 27 (39), 10087-10098
Understanding the role of metal ions in biology can lead to the development of new catalysts for several industrially important transformations. Lanthanides are the most recent group of metal ions that have been shown to be important in biology, that
Publikováno v:
Chemical Science
The separation and recycling of lanthanides is an active area of research with a growing demand that calls for more environmentally friendly lanthanide sources. Likewise, the efficient and industrial separation of lanthanides from the minor actinides
Publikováno v:
European Journal of Inorganic Chemistry. 2021:30-36
Autor:
Alexander Schäfer, Violeta A. Vetsova, Erik K. Schneider, Manfred Kappes, Michael Seitz, Lena J. Daumann, Patrick Weis
Publikováno v:
Journal of the American Society for Mass Spectrometry. 33(4)
Lanthanide-dependent enzymes and their biomimetic complexes have arisen as an interesting target of research in the past decade. These enzymes, specifically, pyrroloquinoline quinone (PQQ)-bearing methanol dehydrogenases, efficiently convert alcohols
Autor:
Sepehr S. Mohammadi, Rob A. Schmitz, Huub J. M. Op den Camp, Mike S. M. Jetten, Arjan Pol, Carmen Hogendoorn, Antonie H. van Gelder, Lena J. Daumann
Publikováno v:
ISME Journal 14 (2020)
ISME Journal, 14, 1223-1232
The ISME Journal
The Isme Journal, 14, pp. 1223-1232
The Isme Journal, 14, 1223-1232
ISME Journal, 14, 1223-1232
The ISME Journal
The Isme Journal, 14, pp. 1223-1232
The Isme Journal, 14, 1223-1232
The trace amounts (0.53 ppmv) of atmospheric hydrogen gas (H2) can be utilized by microorganisms to persist during dormancy. This process is catalyzed by certain Actinobacteria, Acidobacteria, and Chloroflexi, and is estimated to convert 75 × 1012 g
Autor:
Lena J. Daumann, Hurina Hu, N. Cecilia Martinez-Gomez, Huub J. M. Op den Camp, Arjan Pol, Helena Singer, Niko S. W. Jonasson, Bérénice Jahn, Nathan Good
Publikováno v:
Jbic Journal of Biological Inorganic Chemistry, 25, pp. 199-212
JBIC Journal of Biological Inorganic Chemistry
Jbic Journal of Biological Inorganic Chemistry, 25, 199-212
Journal of Biological Inorganic Chemistry
JBIC Journal of Biological Inorganic Chemistry
Jbic Journal of Biological Inorganic Chemistry, 25, 199-212
Journal of Biological Inorganic Chemistry
Methanol dehydrogenases (MDH) have recently taken the spotlight with the discovery that a large portion of these enzymes in nature utilize lanthanides in their active sites. The kinetic parameters of these enzymes are determined with a spectrophotome