Format:
1 Online-Ressource (200 Seiten, 8470 KB)
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Illustrationen, Diagramme
Content:
Iron-sulfur clusters are essential enzyme cofactors. The most common and stable clusters are [2Fe-2S] and [4Fe-4S] that are found in nature. They are involved in crucial biological processes like respiration, gene regulation, protein translation, replication and DNA repair in prokaryotes and eukaryotes. In Escherichia coli, Fe-S clusters are essential for molybdenum cofactor (Moco) biosynthesis, which is a ubiquitous and highly conserved pathway. The first step of Moco biosynthesis is catalyzed by the MoaA protein to produce cyclic pyranopterin monophosphate (cPMP) from 5’GTP. MoaA is a [4Fe-4S] cluster containing radical S-adenosyl-L-methionine (SAM) enzyme. The focus of this study was to investigate Fe-S cluster insertion into MoaA under nitrate and TMAO respiratory conditions using E. coli as a model organism. Nitrate and TMAO respiration usually occur under anaerobic conditions, where oxygen is depleted. Under these conditions, E. coli uses nitrate and TMAO as terminal electron. Previous studies revealed that Fe-S cluster ...
Note:
Dissertation Universität Potsdam 2021
Additional Edition:
Erscheint auch als Druck-Ausgabe Hasnat, Muhammad Abrar, 1989 - A-type carrier proteins are involved in [4Fe-4S] cluster insertion into the radical S-adenosylmethionine (SAM) protein MoaA and other molybdoenzymes Potsdam, 2021
Language:
English
Keywords:
Hochschulschrift
DOI:
10.25932/publishup-53079
URN:
urn:nbn:de:kobv:517-opus4-530791
URL:
https://doi.org/10.25932/publishup-53079
URL:
https://nbn-resolving.org/urn:nbn:de:kobv:517-opus4-530791
URL:
https://d-nb.info/1250335663/34
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