Výsledky vyhledávání - "C. E. Ruggiero"

Evaluation of ovotransferrin-matrix metal-affinity metalloprotein chromatography for Pu(IV) separations

Autor: C. E. Ruggiero, William K. Myers, Mary P. Neu, Sean D. Reilly

Metal-Affinity metalloprotein chromatography has been suggested to have potential for selectively removing actinides from solution. To evaluate this potential, characterization of Pu(IV) and Fe(III) binding to an ovotransferrin-Sepharose™ 4B matrix

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::928c7c6f65a9a9d8bc001f0709621573
https://ora.ox.ac.uk/objects/uuid:b74a8e9a-8daa-4ae8-8b9a-42693c83a563

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Actinide interactions with aerobic soil microbes and their exudates: The reduction of plutonium with desferrioxamine siderophores

Autor: C. E. Ruggiero, J. H. Matonic, M. P. Neu, S. P. Reilly

Publikováno v: AIP Conference Proceedings.

Plutonium is thought to exist mostly as very low soluble and/or strongly sorbed plutonium(IV) hydroxide and oxide species in the environment, and therefore, has low risk of becoming mobile or bioavailable. However, compounds that solubilize plutonium

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::3cad9bf5f121b0a71936ce6b97e99463
https://doi.org/10.1063/1.1292297

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Actinide (Pu, U) interactions with aerobic soil microbes and their exudates: Fundamental chemistry and effects on environmental behavior

Autor: L. A. Vanderberg, M. M. Cox, L.M. He, M. T. Johnson, C. E. Ruggiero, J. R. Fairlee, M. P. Neu, P. D. Gladden, D. J. Chitwood, J. H. Matonic, L. E. Hersman, G. L. Wagner

Publikováno v: AIP Conference Proceedings.

To understand the environmental behavior of metals we must consider a tremendous range of phenomena, from simple individual reactions, such as ligand complexation and solubility equilibria, to quite complicated and collective processes, such as metal

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d70e1cdedc6c8ccfa571b96c92504295
https://doi.org/10.1063/1.1292197

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Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: implications for the biogenesis of topaquinone

Autor: Katsuyuki Tanizawa, J. M. Guss, Matthew C.J. Wilce, William S. McIntire, David M. Dooley, Hans C. Freeman, C. E. Ruggiero, Hideyuki Matsunami, H. Yamaguchi

Publikováno v: Biochemistry. 36(51)

The crystal structures of the copper enzyme phenylethylamine oxidase from the Gram-positive bacterium Arthrobacter globiformis (AGAO) have been determined and refined for three forms of the enzyme: the holoenzyme in its active form (at 2.2 A resoluti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c8c358396f0567dd8a30d66934c8fd5c
https://pubmed.ncbi.nlm.nih.gov/9405045

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