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Keith O. Hodgson
Researcher at Massachusetts Institute of Technology
Publications - 40
Citations - 2860
Keith O. Hodgson is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: Absorption spectroscopy & Ligand. The author has an hindex of 27, co-authored 40 publications receiving 2691 citations. Previous affiliations of Keith O. Hodgson include Technion – Israel Institute of Technology & University of Georgia.
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Journal ArticleDOI
X-ray absorption edge determination of the oxidation state and coordination number of copper: application to the type 3 site in Rhus vernicifera laccase and its reaction with oxygen
Lung Shan Kau,Darlene J. Spira-Solomon,James E. Penner-Hahn,Keith O. Hodgson,Edward I. Solomon +4 more
TL;DR: In this paper, a normalized difference edge analysis is used to quantitatively determine the oxidation states of the copper sites in type 2 copper-depleted (T2D) and native forms of the multicopper oxidase, Rhus vernicifera laccase.
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Electronic structure of the perturbed blue copper site in nitrite reductase: spectroscopic properties, bonding and implications for the entatic/rack state.
Louis B. LaCroix,Susan E. Shadle,Yaning Wang,B. A. Averill,Britt Hedman,Keith O. Hodgson,Edward I. Solomon +6 more
TL;DR: In this article, low-temperature optical absorption, circular dichroism, magnetic circular dichroidism, and sulfur K-edge X-ray absorption spectra have been measured for the green "blue" copper center (type 1) in Achromobacter cycloclastes nitrite reductase.
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Protein Denaturation: A Small-Angle X-ray Scattering Study of the Ensemble of Unfolded States of Cytochrome c†
TL;DR: Solution X-ray scattering was used to study the equilibrium unfolding of cytochrome c as a function of guanidine hydrochloride concentration at neutral pH and reveals the existence of three components, suggesting that at least three equilibrium states of the protein exist.
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Fe L-edge X-ray absorption spectroscopy of low-spin heme relative to non-heme Fe complexes: delocalization of Fe d-electrons into the porphyrin ligand.
Rosalie K. Hocking,Erik C. Wasinger,Yi-Long Yan,Frank M. F. deGroot,F. Ann Walker,Keith O. Hodgson,Britt Hedman,Edward I. Solomon +7 more
TL;DR: A methodology that allows for the interpretation of the multiplet structure of Fe L-edges in terms of differential orbital covalency using a valence bond configuration interaction (VBCI) model is developed and finds that pi-donation to Fe(III) is much larger than pi back-bonding from Fe(II), indicating that a hole superexchange pathway dominates electron transfer.