S
Susan Bailey
Researcher at Daresbury Laboratory
Publications - 17
Citations - 756
Susan Bailey is an academic researcher from Daresbury Laboratory. The author has contributed to research in topics: Reductase & DMSO reductase. The author has an hindex of 11, co-authored 17 publications receiving 715 citations. Previous affiliations of Susan Bailey include Science and Technology Facilities Council & Council for the Central Laboratory of the Research Councils.
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Journal ArticleDOI
Molybdenum Active Centre of Dmso Reductase from Rhodobacter Capsulatus: Crystal Structure of the Oxidised Enzyme at 1.82-A Resolution and the Dithionite-Reduced Enzyme at 2.8-A Resolution
TL;DR: The 1.82-A X-ray crystal structure of the oxidised (Mo(VI)) form of the enzyme dimethylsulfoxide reductase (DMSOR) isolated from Rhodobacter capsulatus is presented in this article.
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Molecular basis of intramolecular electron transfer in sulfite-oxidizing enzymes is revealed by high resolution structure of a heterodimeric complex of the catalytic molybdopterin subunit and A C-type cytochrome subunit
Ulrike Kappler,Susan Bailey +1 more
TL;DR: The structure of the Starkeya novella sulfite dehydrogenase is described, a heterodimeric complex of the catalytic molybdopterin subunit and a c-type cytochrome subunit, that reveals the molecular mechanism of intramolecular electron transfer in sulfite-oxidizing enzymes.
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The crystal and molecular structures of diferric porcine and rabbit serum transferrins at resolutions of 2.15 and 2.60 A, respectively.
TL;DR: The three-dimensional structures of diferric porcine and rabbit serum transferrin have been refined against X-ray diffraction data extending to 2.15 and 2.60 A and the more acid-labile release of iron from serum transferrins than from lactoferrins is discussed.
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Dimethylsulfoxide reductase: an enzyme capable of catalysis with either molybdenum or tungsten at the active site.
Lisa J. Stewart,Lisa J. Stewart,Susan Bailey,Brian Bennett,John M. Charnock,C. David Garner,A. S. McAlpine +6 more
TL;DR: In this paper, it has been shown that tungsten in W-DMSOR is ligated by the dithiolene group of the two pyranopterins, the oxygen atom of Ser147 plus another oxygen atom, and is located in a very similar site to that of molybdenum in Mo-dMSOR, consistent with W L(III)-edge X-ray absorption, EPR and UV/visible spectroscopic data.
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Reversible Dissociation of Thiolate Ligands from Molybdenum in an Enzyme of the Dimethyl Sulfoxide Reductase Family
TL;DR: Evidence is presented that, as a result of O(2) damage, D MSOR samples not submitted to redox-cycling may be contaminated with DMSOR(mod)D and with material absorbing in the region of 400 nm, analogous to the Hepes-modified enzyme.