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of 3
pro vyhledávání: '"Beata M. Wieckowski"'
Hydrogenases are a potential source of environmentally benign bioenergy, using complex cofactors to catalyze the reversible reduction of protons to form hydrogen. The most active subclass, the [FeFe]-hydrogenases, is dependent on a metallocofactor, t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b08d0b6498134de485e3bc6e012cf39d
https://eprints.soton.ac.uk/397330/
https://eprints.soton.ac.uk/397330/
Autor:
Tobias W. Giessen, Leif Flühe, Olaf Burghaus, Mohamed A. Marahiel, Beata M. Wieckowski, Uwe Linne
Publikováno v:
Journal of the American Chemical Society. 135(3)
The sporulation killing factor (SKF) is a 26-residue ribosomally assembled and posttranslationally modified sactipeptide. It is produced by Bacillus subtilis 168 and plays a key role in its sporulation. Like all sactipeptides, SKF contains a thioethe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8995e6fd5add380e27b99c7979eb0cac
https://pubmed.ncbi.nlm.nih.gov/23282011
https://pubmed.ncbi.nlm.nih.gov/23282011
Autor:
Julian D. Hegemann, Olaf Burghaus, Andreas Mielcarek, Beata M. Wieckowski, Mohamed A. Marahiel, Linda Boss
Publikováno v:
FEBS Letters. (15):1802-1806
Thurincin H is a 31-residue, ribosomally synthesized bacteriocin originating from the thn operon of Bacillus thuringiensis SF361. It is the only known sactipeptide carrying four thioether bridges between four cysteines and the α-carbons of a serine,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c86e9c81343951d759b994f990409ec