Lois Geren
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Research Assistant Professor
Also affiliated: University of North Carolina at Chapel Hill (1996–2021); Oklahoma State University (1974–1985); Emory University (1987); University of Illinois Urbana-Champaign (2004–2007); San Diego Supercomputer Center (2002); University of California San Diego (1996); Joint Center for Structural Genomics (2002); University of Texas Health Science Center at Dallas (1986); University of Kansas Medical Center (1975–1977); Rice University (2007); Michigan State University (2002–2008)
Research Areas
Biomedical Subjects
Links
Biography and Research Information
OverviewAI-generated summary
Lois Geren's research focuses on the kinetics and mechanisms of electron transfer in biological systems, particularly involving cytochrome c. Her work investigates the reaction between cytochrome c and cytochrome oxidase, exploring how factors like phosphorylation can regulate this process. Geren has also designed derivatives of cytochrome c, such as a ruthenium-cytochrome c derivative, to specifically measure electron transfer to initial acceptors within cytochrome c oxidase. Her scholarship includes 43 publications with 1,352 citations, and she has an h-index of 23, designating her as a highly cited researcher. Geren has collaborated with several researchers at the University of Arkansas at Fayetteville, including Francis Millett and Bill Durham, on shared publications.
Metrics
- h-index: 23
- Publications: 43
- Citations: 1,360
Positions
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Research Assistant Professor publications 1981–2022University of Arkansas at Fayetteville Institution web page
Selected Publications
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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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Detection of a Proton-Dependent Electron Transfer from CuA to Heme a of Cytochrome C Oxidase Mutant S44e Using Ruthenium Photoexcitation (2010)
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Chapter 28 Use of Ruthenium Photoreduction Techniques to Study Electron Transfer in Cytochrome Oxidase (2009)
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Proton-Dependent Electron Transfer from CuA to Heme a and Altered EPR Spectra in Mutants Close to Heme a of Cytochrome Oxidase (2008)
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C2/2 Rapid kinetic studies of electron transfer in cytochrome oxidase (2008)
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Single-electron photoreduction of the PM intermediate of cytochrome c oxidase (2006)
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Direct measurement of proton release by cytochrome c oxidase in solution during the F→O transition (2004)
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Role of the Conserved Arginine Pair in Proton and Electron Transfer in CytochromecOxidase (2004)
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Mutants of the CuA Site in Cytochrome c Oxidase of Rhodobacter sphaeroides: II. Rapid Kinetic Analysis of Electron Transfer (2002)
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The ins and outs of electrons and protons in cytochrome c oxidase (2000)
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Definition of the Interaction Domain for Cytochrome con Cytochrome c Oxidase (1999)
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Free-Energy Dependence of Electron Transfer in Cytochrome c Labeled with Ruthenium(II)-Polypyridine Complexes (1998)
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Design of a Ruthenium−Cytochrome c Derivative To Measure Electron Transfer to the Radical Cation and Oxyferryl Heme in Cytochrome c Peroxidase (1996)
Collaboration Network
Top Collaborators
- Design of a Ruthenium-Cytochrome c Derivative to Measure Electron Transfer to the Initial Acceptor in Cytochrome c Oxidase
- Photoinduced electron transfer between cytochrome c peroxidase and yeast cytochrome c labeled at Cys 102 with (4-bromomethyl-4'-methylbipyridine)[bis(bipyridine)]ruthenium2+
- Adrenodoxin interaction with adrenodoxin reductase and cytochrome P-450scc. Cross-linking of protein complexes and effects of adrenodoxin modification by 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide.
- Identification of specific carboxylate groups on adrenodoxin that are involved in the interaction with adrenodoxin reductase.
- Fluorescein Isothiocyanate Specifically Modifies Lysine 338 of Cytochrome P-450scc and Inhibits Adrenodoxin Binding
Showing 5 of 28 shared publications
- Design of a Ruthenium-Cytochrome c Derivative to Measure Electron Transfer to the Initial Acceptor in Cytochrome c Oxidase
- Photoinduced electron transfer between cytochrome c peroxidase and yeast cytochrome c labeled at Cys 102 with (4-bromomethyl-4'-methylbipyridine)[bis(bipyridine)]ruthenium2+
- Definition of the Interaction Domain for Cytochrome con Cytochrome c Oxidase
- Role of the Conserved Arginine Pair in Proton and Electron Transfer in CytochromecOxidase
- Design of a Ruthenium−Cytochrome c Derivative To Measure Electron Transfer to the Radical Cation and Oxyferryl Heme in Cytochrome c Peroxidase
Showing 5 of 19 shared publications
- Definition of the Interaction Domain for Cytochrome con Cytochrome c Oxidase
- Role of the Conserved Arginine Pair in Proton and Electron Transfer in CytochromecOxidase
- Mutants of the CuA Site in Cytochrome c Oxidase of Rhodobacter sphaeroides: II. Rapid Kinetic Analysis of Electron Transfer
- Proton-Dependent Electron Transfer from CuA to Heme a and Altered EPR Spectra in Mutants Close to Heme a of Cytochrome Oxidase
- Definition of the Interaction Domain and Electron Transfer Route between Cytochrome c and Cytochrome Oxidase
Showing 5 of 8 shared publications
- Definition of the Interaction Domain for Cytochrome con Cytochrome c Oxidase
- Mutants of the CuA Site in Cytochrome c Oxidase of Rhodobacter sphaeroides: II. Rapid Kinetic Analysis of Electron Transfer
- Definition of the Interaction Domain and Electron Transfer Route between Cytochrome c and Cytochrome Oxidase
- Definition of the Electron Transfer Pathway between Cytochrome c and Cytochrome Oxidase
- The ins and outs of electrons and protons in cytochrome c oxidase
- Definition of the Interaction Domain for Cytochrome con Cytochrome c Oxidase
- Design of a Ruthenium−Cytochrome c Derivative To Measure Electron Transfer to the Radical Cation and Oxyferryl Heme in Cytochrome c Peroxidase
- Mutants of the CuA Site in Cytochrome c Oxidase of Rhodobacter sphaeroides: II. Rapid Kinetic Analysis of Electron Transfer
- The ins and outs of electrons and protons in cytochrome c oxidase
- Design of a Ruthenium-Cytochrome c Derivative to Measure Electron Transfer to the Initial Acceptor in Cytochrome c Oxidase
- Design of a Ruthenium−Cytochrome c Derivative To Measure Electron Transfer to the Radical Cation and Oxyferryl Heme in Cytochrome c Peroxidase
- Identifying the Physiological Electron Transfer Site of Cytochrome c Peroxidase by Structure-Based Engineering
- Free-Energy Dependence of Electron Transfer in Cytochrome c Labeled with Ruthenium(II)-Polypyridine Complexes
- Design of a Ruthenium-Cytochrome c Derivative to Measure Electron Transfer to the Initial Acceptor in Cytochrome c Oxidase
- Design of a Ruthenium−Cytochrome c Derivative To Measure Electron Transfer to the Radical Cation and Oxyferryl Heme in Cytochrome c Peroxidase
- Identifying the Physiological Electron Transfer Site of Cytochrome c Peroxidase by Structure-Based Engineering
- Free-Energy Dependence of Electron Transfer in Cytochrome c Labeled with Ruthenium(II)-Polypyridine Complexes
- Role of the Conserved Arginine Pair in Proton and Electron Transfer in CytochromecOxidase
- Proton-Dependent Electron Transfer from CuA to Heme a and Altered EPR Spectra in Mutants Close to Heme a of Cytochrome Oxidase
- C2/2 Rapid kinetic studies of electron transfer in cytochrome oxidase
- Detection of a Proton-Dependent Electron Transfer from CuA to Heme a of Cytochrome C Oxidase Mutant S44e Using Ruthenium Photoexcitation
- Fluorescein Isothiocyanate Specifically Modifies Lysine 338 of Cytochrome P-450scc and Inhibits Adrenodoxin Binding
- The involvement of carboxylate groups of putidaredoxin in the reaction with putidaredoxin reductase.
- The use of a specific fluorescence probe to study the interaction of adrenodoxin with adrenodoxin reductase and cytochrome P-450scc.
- Identification of specific carboxylate groups on adrenodoxin that are involved in the interaction with adrenodoxin reductase.
- Identification of the binding site on cytochrome c1 for cytochrome c.
- The involvement of carboxylate groups of putidaredoxin in the reaction with putidaredoxin reductase.
- Single-electron photoreduction of the PM intermediate of cytochrome c oxidase
- Accelerated Evolution of Cytochrome c in Higher Primates, and Regulation of the Reaction between Cytochrome c and Cytochrome Oxidase by Phosphorylation
- C2/2 Rapid kinetic studies of electron transfer in cytochrome oxidase
- Single-electron photoreduction of the PM intermediate of cytochrome c oxidase
- Direct measurement of proton release by cytochrome c oxidase in solution during the F→O transition
- C2/2 Rapid kinetic studies of electron transfer in cytochrome oxidase
- Design of a Ruthenium−Cytochrome c Derivative To Measure Electron Transfer to the Radical Cation and Oxyferryl Heme in Cytochrome c Peroxidase
- Electron transfer between cytochromec and cytochromec peroxidase
- Identifying the Physiological Electron Transfer Site of Cytochrome c Peroxidase by Structure-Based Engineering
- Role of the Conserved Arginine Pair in Proton and Electron Transfer in CytochromecOxidase
- Proton-Dependent Electron Transfer from CuA to Heme a and Altered EPR Spectra in Mutants Close to Heme a of Cytochrome Oxidase
- Detection of a Proton-Dependent Electron Transfer from CuA to Heme a of Cytochrome C Oxidase Mutant S44e Using Ruthenium Photoexcitation
- Mutants of the CuA Site in Cytochrome c Oxidase of Rhodobacter sphaeroides: II. Rapid Kinetic Analysis of Electron Transfer
- Definition of the Interaction Domain and Electron Transfer Route between Cytochrome c and Cytochrome Oxidase
- Definition of the Electron Transfer Pathway between Cytochrome c and Cytochrome Oxidase
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