E
Edward I. Solomon
Researcher at Stanford University
Publications - 378
Citations - 26058
Edward I. Solomon is an academic researcher from Stanford University. The author has contributed to research in topics: Active site & Copper. The author has an hindex of 88, co-authored 378 publications receiving 24414 citations. Previous affiliations of Edward I. Solomon include Princeton University & University of California, Davis.
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Journal ArticleDOI
Spectroscopic and Computational Studies of α-Keto Acid Binding to Dke1: Understanding the Role of the Facial Triad and the Reactivity of β-Diketones.
TL;DR: A key role is defined for the 2His/1 carboxylate facial triad in α-keto acid-dependent mononuclear nonheme iron enzymes in stabilizing the bound α- keto acid as a monoanion for its decarboxylation to provide the two additional electrons required for O(2) activation.
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Structure-Function Analysis of the Cuprous Oxidase Activity in Fet3p from Saccharomyces cerevisiae
TL;DR: In this article, the structure of the Fet3 protein was used to identify possible amino acid residues responsible for this protein's reactivity with Cu(I), and structure-function analyses have confirmed this assignment.
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Polarized, single-crystal, electronic spectral studies of hexachlorodicuprate(2-): excited-state effects of binuclear interaction
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Preparation and characterization of a stable half met derivative of type 2 depleted Rhus laccase: Exogenous ligand binding to the type 3 site
Darlene J. Spira,Darlene J. Spira,Marjorie E. Winkler,Marjorie E. Winkler,Edward I. Solomon,Edward I. Solomon +5 more
TL;DR: It is suggested that, in contrast to the well-characterized hemocyanins and tyrosinase coupled binuclear sites, exogenous ligands do not appear to bridge the type 3 binuclear copper ions in laccase.
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Sulfur K-Edge X-ray Absorption Spectroscopy and Density Functional Theory Calculations on Monooxo MoIV and Bisoxo MoVI Bis-dithiolenes: Insights into the Mechanism of Oxo Transfer in Sulfite Oxidase and Its Relation to the Mechanism of DMSO Reductase
TL;DR: Compared with previously studied dimethyl sulfoxide reductase (DMSOr) models, the presence of only one dithiolene at the enzyme active site selectively activates the equatorial oxo for transfer, and allows facile structural reorganization during turnover.