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William E. Antholine
Researcher at Medical College of Wisconsin
Publications - 226
Citations - 9952
William E. Antholine is an academic researcher from Medical College of Wisconsin. The author has contributed to research in topics: Electron paramagnetic resonance & Copper. The author has an hindex of 53, co-authored 226 publications receiving 9476 citations. Previous affiliations of William E. Antholine include Massachusetts Institute of Technology & Chuo University.
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Journal ArticleDOI
Molecular Features of the Copper Binding Sites in the Octarepeat Domain of the Prion Protein
Colin S. Burns,Eliah Aronoff-Spencer,Christine M. Dunham,Paula I. Lario,Nikolai I. Avdievich,William E. Antholine,Marilyn M. Olmstead,Alice Vrielink,Gary J. Gerfen,Jack Peisach,William G. Scott,Glenn L. Millhauser +11 more
TL;DR: The structure reveals an unusual complementary interaction between copper-structured HGGGW units that may facilitate molecular recognition between prion proteins, thereby suggesting a mechanism for transmembrane signaling and perhaps conversion to the pathogenic form.
Journal ArticleDOI
Identification of the Cu2+ Binding Sites in the N-Terminal Domain of the Prion Protein by EPR and CD Spectroscopy
Eliah Aronoff-Spencer,Colin S. Burns,Nikolai I. Avdievich,Gary J. Gerfen,Jack Peisach,William E. Antholine,Haydn L. Ball,Frederick Cohen,Stanley B. Prusiner,Glenn L. Millhauser +9 more
TL;DR: A model consistent with these data is proposed in which Cu(2+) is bound to the nitrogen of the histidine imidazole side chain and to two nitrogens from sequential glycine backbone amides.
Journal ArticleDOI
Nature of the Intermediate Formed in the Reduction of O2 to H2O at the Trinuclear Copper Cluster Active Site in Native Laccase
Sang-Kyu Lee,Serena De Beer George,William E. Antholine,Britt Hedman,Keith O. Hodgson,Edward I. Solomon +5 more
TL;DR: The native intermediate appears to be the catalytically relevant fully oxidized form of the enzyme, and its role in catalysis is considered.
Journal ArticleDOI
Copper coordination in the full-length, recombinant prion protein.
Colin S. Burns,Eliah Aronoff-Spencer,Giuseppe Legname,Stanley B. Prusiner,William E. Antholine,Gary J. Gerfen,Jack Peisach,Glenn L. Millhauser +7 more
TL;DR: Rec recombinant, full-length Syrian hamster PrP is investigated using EPR methodologies and quantification studies reveal a fifth binding site in the flexible region between the octarepeats and the PrP globular C-terminal domain, which seems to provide a complete profile of the copper binding sites in PrP.
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Chromium(VI) reductase activity is associated with the cytoplasmic membrane of anaerobically grown Shewanella putrefaciens MR-1.
TL;DR: Formate‐dependent Cr(VI) reductase activity was detected in anaerobically grown cells of S. putrefaciens MR‐1, with highest specific activity in the cytoplasmic membrane, suggesting involvement of a multi‐component electron transport chain which could include cytochromes and quinones.