Francis Millett
Affiliation confirmed via AI analysis of OpenAlex, ORCID, and web sources.
Professor
Also affiliated: University of North Carolina at Chapel Hill (2021); Goethe University Frankfurt (2008); Oklahoma State University (1985–2007); University of Hawaiʻi at Mānoa (1996); California Institute of Technology (1972–1974); Texas Tech University (1987); Monsanto (United States) (1999); St. Jude Children's Research Hospital (1981); University of Hawaii System (1996); University of Wisconsin–Madison (1966); Emory University (1987); University of Illinois Urbana-Champaign (1998–2007); University of New Mexico (1996); University of Oregon (1982); San Diego Supercomputer Center (2002); University of L'Aquila (2008); University of Arkansas System (1993–1994); United States Public Health Service (1978); Joint Center for Structural Genomics (2002); University of Texas Health Science Center at Dallas (1986); La Roche College (1981); Rice University (2007); Columbia University (1969–1972); Michigan State University (2002–2008)
Faculty Researcher
Research Areas
Biomedical Subjects
Links
Biography and Research Information
OverviewAI-generated summary
Francis Millett, a professor at the University of Arkansas at Fayetteville, studies electron transfer mechanisms in biological systems, particularly focusing on cytochrome proteins. His recent work investigates the dynamics of the iron-sulfur protein in the cytochrome bc1 complex during bifurcated electron transfer. Millett has also examined the evolutionary changes in cytochrome c among higher primates and explored how phosphorylation regulates the reaction between cytochrome c and cytochrome oxidase.
Further research includes the design of ruthenium-cytochrome c derivatives to measure electron transfer to initial acceptors in cytochrome c oxidase. Millett leads an active research group and collaborates with other researchers at the University of Arkansas, including Bill Durham, Lois Geren, Martha Scharlau, and Clayre Parson. He has an h-index of 42 with 4,776 total citations across 144 publications, and has been recognized as a highly cited researcher.
Metrics
- h-index: 42
- Publications: 144
- Citations: 4,784
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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The Effect of Multiple Phosphorylations on the Interaction between Cytochrome C and Cytochrome C Oxidase (2020)
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Regulation of Electron Transfer from Cytochrome C to Cytochrome C Oxidase by Phosphorylation of CC THR-28 (2020)
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Determination of the Binding Interaction between Mitochondrial Electron Transport Chain Proteins Cytochrome C and Cytochrome C Oxidase (2020)
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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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Regulation of the Reaction between Cytochrome c and Cytochrome Oxidase (2016)
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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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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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Synthesis and characterization of Cr(III), Mn(II), Co(II), Ni(II), and Cu(II) complexes with a hexadentate hemi-cage ligand formed with bipyridine (2010)
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Chapter 5 Use of Ruthenium Photooxidation Techniques to Study Electron Transfer in the Cytochrome bc1 Complex (2009)
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Chapter 28 Use of Ruthenium Photoreduction Techniques to Study Electron Transfer in Cytochrome Oxidase (2009)
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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