Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Christoph, Laurich"'
Autor:
Joern Krausze, Eduard J. Reijerse, Wolfgang Lubitz, Christoph Laurich, Juergen Moser, Dieter Jahn, Marco Massmig
Publikováno v:
'Journal of Biological Chemistry ', vol: 295, pages: 13065-13078 (2020)
Bacterial formation of trimethylamine (TMA) from carnitine in the gut microbiome has been linked to cardiovascular disease. During this process, the two-component carnitine monooxygenase (CntAB) catalyzes the oxygen-dependent cleavage of carnitine to
Autor:
Marco, Massmig, Edward, Reijerse, Joern, Krausze, Christoph, Laurich, Wolfgang, Lubitz, Dieter, Jahn, Jürgen, Moser
Publikováno v:
J Biol Chem
Bacterial formation of trimethylamine (TMA) from carnitine in the gut microbiome has been linked to cardiovascular disease. During this process, the two-component carnitine monooxygenase (CntAB) catalyzes the oxygen-dependent cleavage of carnitine to
Publikováno v:
Biochemistry. 55:4344-4355
Iron-sulfur clusters form one of the largest and most diverse classes of enzyme cofactors in nature. They may serve as structural factors, form electron transfer chains between active sites and external redox partners, or form components of enzyme ac
Autor:
Marc Stassen, Nicole Frankenberg-Dinkel, Michael Rother, Samir F. El-Mashtoly, Christoph Laurich, Bastian Molitor, John H. Dawson, Anuja Modi, Wolfgang Lubitz
Publikováno v:
Journal of Biological Chemistry. 288:18458-18472
Based on a bioinformatics study, the protein MA4561 from the methanogenic archaeon Methanosarcina acetivorans was originally predicted to be a multidomain phytochrome-like photosensory kinase possibly binding open-chain tetrapyrroles. Although we wer
Autor:
Christoph Laurich, Dagmar Rother, Edward J. Reijerse, Petra Hellwig, Wolfgang Lubitz, Monika Sommerhalter, Eberhard Bothe, Cornelius G. Friedrich, Armin Quentmeier
Publikováno v:
Biochemistry. 46:7804-7810
The heterodimeric hemoprotein SoxXA, essential for lithotrophic sulfur oxidation of the aerobic bacterium Paracoccus pantotrophus, was examined by a combination of spectroelectrochemistry and EPR spectroscopy. The EPR spectra for SoxXA showed contrib
Autor:
Bartosz Szyszko, Gudrun Klihm, Klaus Möbius, Christoph Laurich, Marcin Stępień, Anton Savitsky, Lechosław Latos-Grażyński, Martin Plato, Wolfgang Lubitz
The symmetry of the arrangement of objects has fascinated philosophers, artists and scientists for a long time, and still does. Symmetries often exist in nature, but are also created artificially, for instance by chemical synthesis of novel molecules
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b54a7b1b4ea2ae80e83c3b80297305f
https://refubium.fu-berlin.de/handle/fub188/15004
https://refubium.fu-berlin.de/handle/fub188/15004
Publikováno v:
Biochemistry. 45:9706-9716
The active site in the [NiFe] hydrogenase of Desulfovibrio vulgaris Miyazaki F has been investigated by Fourier transform infrared (FTIR) spectroscopy. Analysis of the spectra allowed the three diatomic inorganic ligands to Fe in this enzyme to be id