J
James Terner
Researcher at Virginia Commonwealth University
Publications - 75
Citations - 3714
James Terner is an academic researcher from Virginia Commonwealth University. The author has contributed to research in topics: Resonance Raman spectroscopy & Raman spectroscopy. The author has an hindex of 34, co-authored 74 publications receiving 3520 citations. Previous affiliations of James Terner include University of North Carolina at Chapel Hill & Centre national de la recherche scientifique.
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Journal ArticleDOI
Microwave synthesis of graphene sheets supporting metal nanocrystals in aqueous and organic media
Hassan M.A. Hassan,Victor Abdelsayed,Abd El Rahman S. Khder,Khaled M. AbouZeid,James Terner,M. Samy El-Shall,Saud I. Al-Resayes,A. A. El-Azhary +7 more
TL;DR: In this article, a facile and scalable chemical reduction method assisted by microwave irradiation for the synthesis of chemically converted graphene sheets and metal nanoparticles dispersed on the graphene sheets was developed.
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The crystal structure of chloroperoxidase: a heme peroxidase--cytochrome P450 functional hybrid.
TL;DR: The structure determination of CPO was undertaken to help elucidate those structural features that enable the enzyme to exhibit these multiple activities of peroxidase, catalase and cytochrome P450-like activities in addition to catalyzing halogenation reactions.
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Ultrasmall gold nanoparticles anchored to graphene and enhanced photothermal effects by laser irradiation of gold nanostructures in graphene oxide solutions.
TL;DR: The Au nanostructures/graphene oxide solutions and the ultrasmall gold- graphene nanocomposites are proposed as promising materials for photothermal therapy and for the efficient conversion of solar energy into usable heat for a variety of thermal, thermochemical, and thermomechanical applications.
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Stereochemistry of the chloroperoxidase active site: crystallographic and molecular-modeling studies
TL;DR: Molecular modeling and dynamics simulations of CPO with the substrate cis-beta methylstyrene and the corresponding epoxide products provide a structural and energetic basis for understanding the enantioselectivity of C PO-catalyzed epoxidation reactions.
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Heme-linked ionization of horseradish peroxidase compound II monitored by the resonance Raman Fe(IV)=O stretching vibration.
TL;DR: It is shown that Fe(IV)=O stretching frequency for horseradish peroxidase compound II will switch between two values depending on pH, with pKa values corresponding to the previously reported compound II heme-linked ionizations.