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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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Spectroscopic Studies of Perturbed T1 Cu Sites in the Multicopper Oxidases Saccharomyces cerevisiae Fet3p and Rhus vernicifera Laccase: Allosteric Coupling between the T1 and Trinuclear Cu Sites†

TL;DR: Spectroscopic methods show that vibrations in the cysteine side chain of the T1 Cu site and the protein backbone couple to the Cu-S vibration provide a possible mechanism for regulating intramolecular T1 to TNC ET in NI and partially reduced enzyme forms for efficient turnover.
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Heme-copper-dioxygen complexes: toward understanding ligand-environmental effects on the coordination geometry, electronic structure, and reactivity.

TL;DR: A geometric structure and more complete electronic description of the high-spin heme-peroxo-copper complexes 1 and 2 and the phenoxyl radical generated by the H-atom abstraction was either directly detected by electron paramagnetic resonance spectroscopy using phenols that produce stable radicals or indirectly detected by the coupling product of two Phenoxyl radicals.
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Hydroxo-bridged dicopper(II,III) and -(III,III) complexes: models for putative intermediates in oxidation catalysis.

TL;DR: A macrocyclic ligand (L4–) comprising two pyridine(dicarboxamide) donors was used to target reactive copper species relevant to proposed intermediates in catalytic hydrocarbon oxidations by particulate methane monooxygenase and heterogeneous zeolite systems to provide the first precedence for such moieties as oxidation catalysis intermediates.
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Activation of α-Keto Acid-Dependent Dioxygenases: Application of an {FeNO}7/{FeO2}8 Methodology for Characterizing the Initial Steps of O2 Activation

TL;DR: In this study, NO is used as an O(2) analogue to probe the effects of α-keto acid binding in 4-hydroxyphenylpyruvate dioxygenase (HPPD) and a combination of EPR, UV-vis absorption, magnetic circular dichroism (MCD), and variable-temperature, variable-field (VTVH) MCD spectroscopies in conjunction with computational models are used.
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Nuclear Resonance Vibrational Spectroscopy on the FeIVO S=2 Non-Heme Site in TMG3tren: Experimentally Calibrated Insights into Reactivity

TL;DR: These studies define the steric and intrinsic electronic contributions to the reaction barriers and establish that both the S = 1 and S = 2 surfaces have significant steric contributions due to the different directionalities of substrate approach and thus similar intrinsic reactivities.