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Arthur Oubrie
Researcher at University of East Anglia
Publications - 32
Citations - 1059
Arthur Oubrie is an academic researcher from University of East Anglia. The author has contributed to research in topics: Active site & Pyrroloquinoline quinone. The author has an hindex of 15, co-authored 30 publications receiving 1007 citations. Previous affiliations of Arthur Oubrie include University of Groningen & Merck & Co..
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Nitric oxide reductases in bacteria
Janneke Hendriks,Arthur Oubrie,Jose Castresana,Andrea Urbani,Sabine Gemeinhardt,Matti Saraste +5 more
TL;DR: The current knowledge on bacterial NORs is summarized, the evolutionary relationship between them and cytochrome oxidases is discussed, and two types ofacterial NORs have been characterised.
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Structure and mechanism of soluble quinoprotein glucose dehydrogenase.
Arthur Oubrie,Henriëtte J. Rozeboom,Kor H. Kalk,Arjen J. J. Olsthoorn,Johannis A. Duine,Bauke W. Dijkstra +5 more
TL;DR: In this article, the X-ray structure of s-GDH with the cofactor pyrroloquinoline quinone (PQQ) was determined at 2.2 A resolution and a complex with reduced PQQ and glucose at 1.9 A resolution.
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Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni: structural basis for substrate oxidation and electron transfer.
TL;DR: This is the first reported structure of an electron transfer system between a quinoprotein alcohol dehydrogenase and cytochrome c and one of the longest physiological edge-to-edge distances yet determined between two redox centers.
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The 1.7 A crystal structure of the apo form of the soluble quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus reveals a novel internal conserved sequence repeat.
TL;DR: A data base search unexpectedly showed that four uncharacterized protein sequences are homologous to s-GDH with many residues in the putative active site absolutely conserved, indicating that these homologs may have a similar structure and that they may catalyze similar PQQ-dependent reactions.
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Signal peptide–chaperone interactions on the twin-arginine protein transport pathway
Kostas Hatzixanthis,Thomas A. Clarke,Arthur Oubrie,David J. Richardson,Raymond J. Turner,Frank Sargent +5 more
TL;DR: It is demonstrated here that purified TorD binds tightly and with exquisite specificity to the TorA twin-arginine signal peptide in vitro, and it is reported that the TorD family constitutes a hitherto unexpected class of nucleotide-binding proteins.