Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Anton Brausemann"'
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-10 (2023)
Abstract Mono- and multiheme cytochromes c are post-translationally matured by the covalent attachment of heme. For this, Escherichia coli employs the most complex type of maturation machineries, the Ccm-system (for cytochrome c maturation). It consi
Externí odkaz:
https://doaj.org/article/9b48aaf891444375adde52747b35de59
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
Abstract Latex clearing proteins (Lcps) are rubber oxygenases that catalyse the extracellular cleavage of poly (cis-1,4-isoprene) by Gram-positive rubber degrading bacteria. Lcp of Streptomyces sp. K30 (LcpK30) is a b-type cytochrome and acts as an e
Externí odkaz:
https://doaj.org/article/532ad933220c47fabfed16e8602af9ad
Autor:
Julian Koschmieder, Mirjam Fehling-Kaschek, Patrick Schaub, Sandro Ghisla, Anton Brausemann, Jens Timmer, Peter Beyer
Publikováno v:
PLoS ONE, Vol 12, Iss 11, p e0187628 (2017)
Phytoene desaturase (PDS) is an essential plant carotenoid biosynthetic enzyme and a prominent target of certain inhibitors, such as norflurazon, acting as bleaching herbicides. PDS catalyzes the introduction of two double bonds into 15-cis-phytoene,
Externí odkaz:
https://doaj.org/article/fab7c6b6c59e40b29afa1ab954c711d6
Autor:
Sandra Gemmecker, Patrick Schaub, Julian Koschmieder, Anton Brausemann, Friedel Drepper, Marta Rodriguez-Franco, Sandro Ghisla, Bettina Warscheid, Oliver Einsle, Peter Beyer
Publikováno v:
PLoS ONE, Vol 10, Iss 7, p e0131717 (2015)
Recombinant phytoene desaturase (PDS-His6) from rice was purified to near-homogeneity and shown to be enzymatically active in a biphasic, liposome-based assay system. The protein contains FAD as the sole protein-bound redox-cofactor. Benzoquinones, n
Externí odkaz:
https://doaj.org/article/9bd68630961b416e8aeb0a57ddca2f2e
Publikováno v:
Nature Chemical Biology. 17:800-805
The covalent attachment of one or multiple heme cofactors to cytochrome c protein chains enables cytochrome c proteins to be used in electron transfer and redox catalysis in extracytoplasmic environments. A dedicated heme maturation machinery, whose
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::949e69d06b4449e1c6242b5bab4e46d9
https://doi.org/10.1038/s41589-021-00793-8
https://doi.org/10.1038/s41589-021-00793-8
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
Scientific Reports
Scientific Reports
Latex clearing proteins (Lcps) are rubber oxygenases that catalyse the extracellular cleavage of poly (cis-1,4-isoprene) by Gram-positive rubber degrading bacteria. Lcp of Streptomyces sp. K30 (LcpK30) is a b-type cytochrome and acts as an endo-type
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1466918fa57e54a4ad54ffcc54b93c40
https://doaj.org/article/532ad933220c47fabfed16e8602af9ad
https://doaj.org/article/532ad933220c47fabfed16e8602af9ad
Publikováno v:
FEBS letters. 591(12)
Geobacter sulfurreducens is a dissimilatory metal reducing bacterium with notable properties and significance in biotechnological applications. Biochemical studies suggest that the inner membrane-associated diheme cytochrome MacA and the periplasmic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::781cfe943903fffca80406a54bfad954
https://pubmed.ncbi.nlm.nih.gov/28542725
https://pubmed.ncbi.nlm.nih.gov/28542725
Publikováno v:
Heme Peroxidases ISBN: 9781849739115
Bacterial diheme peroxidases (bCCP) act in the detoxification of reactive oxygen species by reduction of peroxide to water. The substrate H2O2 is bound to the free axial position of a heme cofactor, and in a first step, one H2O molecule is released,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b8accba72ebb4088c932077621243a55
https://doi.org/10.1039/9781782622628-00113
https://doi.org/10.1039/9781782622628-00113
Autor:
Stefan Gerhardt, Anton Brausemann, Nils Johnsson, Anne-Kathrin Schott, Thomas Gronemeyer, Andreas Große-Berkenbusch, Oliver Einsle
Publikováno v:
Journal of structural biology. 193(3)
Septins are a conserved family of GTP-binding proteins that assemble into a highly ordered array of filaments at the mother bud neck in Saccharomyces cerevisiae cells. Many molecular functions and mechanisms of the septins in S. cerevisiae were alrea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b927f472179c714e256a54586652dfc9
https://pubmed.ncbi.nlm.nih.gov/26780475
https://pubmed.ncbi.nlm.nih.gov/26780475
Autor:
Marta Rodriguez-Franco, Julian Koschmieder, Patrick Schaub, Peter Beyer, Oliver Einsle, Bettina Warscheid, Friedel Drepper, Sandra Gemmecker, Sandro Ghisla, Anton Brausemann
Publikováno v:
PLoS ONE
PLoS ONE, Vol 10, Iss 7, p e0131717 (2015)
PLoS ONE, Vol 10, Iss 7, p e0131717 (2015)
Recombinant phytoene desaturase (PDS-His6) from rice was purified to near-homogeneity and shown to be enzymatically active in a biphasic, liposome-based assay system. The protein contains FAD as the sole protein-bound redox-cofactor. Benzoquinones, n
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17924ca0ea97ca1e81b0f9304e59213c
http://europepmc.org/articles/PMC4492965
http://europepmc.org/articles/PMC4492965