# positions[].organizations[].parent[].label
College of Agriculture and Life Sciences

# overview
Oxidoreductases use metallocofactors, organic molecules, and four amino acids (Tyr, Trp, Cys, and Gly) to perform electron transfer (ET) and proton-coupled electron transfer (PCET) reactions. These four amino acids serve as one-electron (radical) redox mediators in biocatalytic and multistep electron/hole transfer processes, some of which are essential to life on earth. There is also a sinister side to amino-acid ET/PCET since these reactions can be induced at oxidative stress conditions and cause significant cellular damage. It is extremely challenging to experimentally resolve the thermodynamic and kinetic redox properties of a single amino-acid residue. Consequently, key information to support the understanding of one of nature's essential redox tools is missing. Our research focuses on developing a family of well-structured model proteins with the unique capability of providing detailed mechanistic information on Tyr (Y) and Trp (W) oxidation-reduction reactions.

# keywords[]
Photosynthetic Reaction Center Complex Proteins

# keywords[]
Photosynthetic Reaction Center Complex Proteins

# keywords[]
Photosynthetic Reaction Center Complex Proteins

# keywords[]
Photosynthetic Reaction Center Complex Proteins

# keywords[]
3407 Theoretical And Computational Chemistry

# keywords[]
Immobilized Metal Ion Affinity Chromatography

# keywords[]
Photosynthetic Reaction Center Complex Proteins

# keywords[]
Photosynthetic Reaction Center Complex Proteins

# educationAndTraining[].organization.label
Stockholm University - (Stockholm, Sweden)

# educationAndTraining[].organization.label
Stockholm University - (Stockholm, Sweden)

# publications[].label
Formal Reduction Potentials of Difluorotyrosine and Trifluorotyrosine Protein Residues: Defining the Thermodynamics of Multistep Radical Transfer.

# publications[].label
Reversible voltammograms and a Pourbaix diagram for a protein tyrosine radical.

# publications[].publisher
Proceedings of the National Academy of Sciences

# publications[].label
Properties of Site-Specifically Incorporated 3-Aminotyrosine in Proteins To Study Redox-Active Tyrosines: Escherichia coli Ribonucleotide Reductase as a Paradigm.

# publications[].label
De novo proteins as models of radical enzymes.

# publications[].label
Redox characteristics of a de novo quinone protein.

# publications[].label
Modified EPR spectra of the tyrosineD radical in photosystem II in site-directed mutants of Synechocystis sp. PCC 6803: identification of side chains in the immediate vicinity of tyrosineD on the D2 protein.

# publications[].label
Solution structure of the core SMN-Gemin2 complex.

# publications[].label
Improving yields of deuterated, methyl labeled protein by growing in H2O.

# publications[].label
Formal reduction potential of 3,5-difluorotyrosine in a structured protein: insight into multistep radical transfer.

# publications[].label
Proton and hydrogen currents in photosynthetic water oxidation.

# publications[].label
Proton-Coupled Electron Transfer upon Oxidation of Tyrosine in a De Novo Protein: Analysis of Proton Acceptor Candidates.

# publications[].label
Electron, proton and hydrogen-atom transfers in photosynthetic water oxidation.

# publications[].label
Exploring amino-acid radical chemistry: protein engineering and de novo design.

# publications[].label
Forced folding and structural analysis of metastable proteins.

# publications[].label
Making a single-chain four-helix bundle for redox chemistry studies.

# publications[].label
Structure of a de novo designed protein model of radical enzymes.

# publications[].label
Switching the proton-coupled electron transfer mechanism for non-canonical tyrosine residues in a de novo protein.

# publications[].label
A Quick and Colorful Method to Measure Low-Level Contaminations of Paramagnetic Ni2+ in Protein Samples Purified by Immobilized Metal Ion Affinity Chromatography.

# publications[].label
Computing Proton-Coupled Redox Potentials of Fluorotyrosines in a Protein Environment.

# publications[].label
Manganese and tyrosyl radical function in photosynthetic oxygen evolution.

# publications[].label
Pourbaix Diagram, Proton-Coupled Electron Transfer, and Decay Kinetics of a Protein Tryptophan Radical: Comparing the Redox Properties of W32 and Y32 Generated Inside the Structurally Characterized 3W and 3Y Proteins.

# publications[].label
Reversible phenol oxidation and reduction in the structurally well-defined 2-Mercaptophenol-C protein.

# publications[].label
A >200 meV Uphill Thermodynamic Landscape for Radical Transport in Escherichia coli Ribonucleotide Reductase Determined Using Fluorotyrosine-Substituted Enzymes.

# publications[].label
Point-mutations affecting the properties of tyrosineD in photosystem II. Characterization by isotopic labeling and spectral simulation.

# publications[].label
Environmental modulation of protein cation-pi interactions.

# publications[].label
Tyrosyl radicals in enzyme catalysis: some properties and a focus on photosynthetic water oxidation.

# publications[].label
Photochemical tyrosine oxidation in the structurally well-defined 3Y protein: proton-coupled electron transfer and a long-lived tyrosine radical.

# publications[].label
Protease-stable DARPins as promising oral therapeutics.

# publications[].label
Moving a phenol hydroxyl group from the surface to the interior of a protein: effects on the phenol potential and pK(A).

# publications[].label
The function and characteristics of tyrosyl radical cofactors.

# publications[].label
Electrochemical and structural properties of a protein system designed to generate tyrosine Pourbaix diagrams.

# publications[].label
Insights into the Thermodynamics and Kinetics of Amino-Acid Radicals in Proteins.

# publications[].label
A hydrogen-atom abstraction model for the function of YZ in photosynthetic oxygen evolution.

# publications[].label
Defining the Apoptotic Trigger: THE INTERACTION OF CYTOCHROME c AND CARDIOLIPIN.

# publications[].label
Proton-Coupled Electron Transfer from Tyrosine in the Interior of a de novo Protein: Mechanisms and Primary Proton Acceptor.

# publications[].label
Concerted hydrogen-atom abstraction in photosynthetic water oxidation.

# organizations[]
College of Agriculture and Life Sciences

# schools[]
College of Agriculture and Life Sciences