Bill Durham
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Researcher
Also affiliated: Goethe University Frankfurt (2008); Oklahoma State University (2000–2012); Lawrence Livermore National Laboratory (2006); Monsanto (United States) (1999); National Oceanic and Atmospheric Administration (2002); University of Leeds (2012); Agricultural Research Service (2017); National Institute of Standards and Technology (2002); University of Illinois Urbana-Champaign (1998–2007); Cooperative Institute for Research in Environmental Sciences (2002); University of Georgia (2002); University of North Carolina at Greensboro (1988); San Diego Supercomputer Center (2002); Wayne State University (1979); University of Colorado Boulder (2002); Clarkson College (1974); University of L'Aquila (2008); University of Arkansas System (1993–1994); Idaho National Laboratory (2006); University at Albany, State University of New York (2002); Joint Center for Structural Genomics (2002); Phoenix Integration (United States) (2012); Yankee Environmental System (United States) (2002); Biospherical Instruments (United States) (2002); Smithsonian Environmental Research Center (2002); Rice University (2007); Michigan State University (2002–2008); Colorado State University (2002–2009)
Faculty Researcher
Research Areas
Biomedical Subjects
Biography and Research Information
OverviewAI-generated summary
Bill Durham's research focuses on the study of electron transfer processes, particularly within biological systems such as cytochrome c and cytochrome oxidase. His work investigates the dynamics of protein rotation during bifurcated electron transfer and explores the regulation of reactions between these proteins, including the impact of phosphorylation. Durham has also designed molecular constructs, such as ruthenium-cytochrome c derivatives, to probe specific electron transfer events.
His scholarship includes 158 publications with over 4,300 citations, and an h-index of 37. Durham has collaborated with several researchers at the University of Arkansas at Fayetteville, including Francis Millett, Lois Geren, Martha Scharlau, and Clayre Parson. His recent publications demonstrate an ongoing engagement with the fundamental mechanisms of electron transport and protein interactions in biological contexts.
Metrics
- h-index: 37
- Publications: 158
- Citations: 4,374
Selected Publications
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Photoinduced electron transfer in cytochrome bc1: Dynamics of rotation of the Iron-sulfur protein during bifurcated electron transfer from ubiquinol to cytochrome c1 and cytochrome bL (2023)
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Accelerated Evolution of Cytochrome c in Higher Primates, and Regulation of the Reaction between Cytochrome c and Cytochrome Oxidase by Phosphorylation (2022)
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Definition of the Interaction Domain and Electron Transfer Route between Cytochrome c and Cytochrome Oxidase (2019)
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Definition of the Electron Transfer Pathway between Cytochrome c and Cytochrome Oxidase (2018)
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Proteo-lipobeads for the oriented encapsulation of membrane proteins (2015)
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Gas chromatography–mass spectrometry of JWH-018 metabolites in urine samples with direct comparison to analytical standards (2013)
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Design and use of photoactive ruthenium complexes to study electron transfer within cytochrome bc1 and from cytochrome bc1 to cytochrome c (2012)
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Rapid characterization of lipids by MALDI MS. Part 2: Artifacts, ion suppression, and TLC MALDI imaging (2012)
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Ruthenium Photoinitiation of Electron Transfer in the Rb. Sphaeroides Cytochrome bc1 Complex: Rotational dynamics of the iron-sulfur protein, diffusion of quinone between the Qo and Qi sites, and linkage between the two monomers (2012)
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Geologic nitrogen and climate change in the geochemical budget of Kärkevagge, Swedish Lapland (2012)
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Rapid characterization of lipids by MALDI MS. Part 1: Bacterial taxonomy and analysis of food oils (2012)
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Design of photoactive ruthenium complexes to study electron transfer and proton pumping in cytochrome oxidase (2011)
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Photoinitiated Electron Transfer within the <i>Paracoccus denitrificans</i> Cytochrome <i>bc</i><sub>1</sub> Complex: Mobility of the Iron–Sulfur Protein Is Modulated by the Occupant of the Q<sub>o</sub> Site (2011)
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The acidic domain of cytochrome c1 in Paracoccus denitrificans, analogous to the acidic subunits in eukaryotic bc1 complexes, is not involved in the electron transfer reaction to its native substrate cytochrome c552 (2011)
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Laser Desorption/Ionization Time‐of‐Flight Mass Spectrometry of Triacylglycerols and Other Components in Fingermark Samples* (2011)
Collaboration Network
Top Collaborators
- Accelerated Evolution of Cytochrome c in Higher Primates, and Regulation of the Reaction between Cytochrome c and Cytochrome Oxidase by Phosphorylation
- Photoinduced electron transfer in cytochrome bc1: Dynamics of rotation of the Iron-sulfur protein during bifurcated electron transfer from ubiquinol to cytochrome c1 and cytochrome bL
- Accelerated Evolution of Cytochrome c in Higher Primates, and Regulation of the Reaction between Cytochrome c and Cytochrome Oxidase by Phosphorylation
- Accelerated Evolution of Cytochrome c in Higher Primates, and Regulation of the Reaction between Cytochrome c and Cytochrome Oxidase by Phosphorylation
- Accelerated Evolution of Cytochrome c in Higher Primates, and Regulation of the Reaction between Cytochrome c and Cytochrome Oxidase by Phosphorylation
- Accelerated Evolution of Cytochrome c in Higher Primates, and Regulation of the Reaction between Cytochrome c and Cytochrome Oxidase by Phosphorylation
- Accelerated Evolution of Cytochrome c in Higher Primates, and Regulation of the Reaction between Cytochrome c and Cytochrome Oxidase by Phosphorylation
- Accelerated Evolution of Cytochrome c in Higher Primates, and Regulation of the Reaction between Cytochrome c and Cytochrome Oxidase by Phosphorylation
- Accelerated Evolution of Cytochrome c in Higher Primates, and Regulation of the Reaction between Cytochrome c and Cytochrome Oxidase by Phosphorylation
- Accelerated Evolution of Cytochrome c in Higher Primates, and Regulation of the Reaction between Cytochrome c and Cytochrome Oxidase by Phosphorylation
- Accelerated Evolution of Cytochrome c in Higher Primates, and Regulation of the Reaction between Cytochrome c and Cytochrome Oxidase by Phosphorylation
- Photoinduced electron transfer in cytochrome bc1: Dynamics of rotation of the Iron-sulfur protein during bifurcated electron transfer from ubiquinol to cytochrome c1 and cytochrome bL
- Photoinduced electron transfer in cytochrome bc1: Dynamics of rotation of the Iron-sulfur protein during bifurcated electron transfer from ubiquinol to cytochrome c1 and cytochrome bL
- Photoinduced electron transfer in cytochrome bc1: Dynamics of rotation of the Iron-sulfur protein during bifurcated electron transfer from ubiquinol to cytochrome c1 and cytochrome bL
- Photoinduced electron transfer in cytochrome bc1: Dynamics of rotation of the Iron-sulfur protein during bifurcated electron transfer from ubiquinol to cytochrome c1 and cytochrome bL
- Photoinduced electron transfer in cytochrome bc1: Dynamics of rotation of the Iron-sulfur protein during bifurcated electron transfer from ubiquinol to cytochrome c1 and cytochrome bL
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