ArticleACS chemical biology2010
Control of proton and electron transfer in de novo designed, biomimetic β hairpins.
Article in ACS chemical biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 29 citations in OpenAlex.
- Modulating Radical Propagation in Proteins by Proton-Coupled Electron Transfer and Hydrogen Bonding.Biochemistry · 2026Article
- A Triangulenum-Based Biosensor Platform for Mapping Kinase Activity in T Cells.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- ChlorophyllPlants (Basel, Switzerland) · 2026Article
- Origins of the Intrinsic Redox Activity of Biomolecular Condensates.Journal of the American Chemical Society · 2026Article
- Electrochemical and Structural Study of the Buried Tryptophan in Azurin: Effects of Hydration and Polarity on the Redox Potential of W48.The journal of physical chemistry. B · 2023Article
- Specific metallo-protein interactions and antimicrobial activity in Histatin-5, an intrinsically disordered salivary peptide.Scientific reports · 2019Article
- Structure and Function of Tryptophan-Tyrosine Dyads in Biomimetic β Hairpins.The journal of physical chemistry. B · 2019Article
- Proton-coupled electron hopping in Ru-modified P. aeruginosa azurin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Article
- A tyrosine-tryptophan dyad and radical-based charge transfer in a ribonucleotide reductase-inspired maquette.Nature communications · 2015Article
- Moving protons and electrons in biomimetic systems.Biochemistry · 2015Review
- Hydrogen bond network between amino acid radical intermediates on the proton-coupled electron transfer pathway of E. coli α2 ribonucleotide reductase.Journal of the American Chemical Society · 2015Article
- Reversible voltammograms and a Pourbaix diagram for a protein tyrosine radical.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Redox properties of tyrosine and related molecules.FEBS letters · 2012Review
- Proton Coupled Electron Transfer and Redox Active Tyrosines: Structure and Function of the Tyrosyl Radicals in Ribonucleotide Reductase and Photosystem II.The journal of physical chemistry letters · 2012Article
- Photo-ribonucleotide reductase β2 by selective cysteine labeling with a radical phototrigger.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Electrochemical and structural properties of a protein system designed to generate tyrosine Pourbaix diagrams.Journal of the American Chemical Society · 2011Article
- Proton coupled electron transfer and redox active tyrosines in Photosystem II.Journal of photochemistry and photobiology. B, BiologyReview
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Tyrosine side chains are involved in proton coupled electron transfer reactions (PCET) in many complex proteins, including photosystem II (PSII) and ribonucleotide reductase. For example, PSII contains two redox-active tyrosines, TyrD (Y160D2) and TyrZ (Y161D1), which have different protein environments, midpoint potentials, and roles in catalysis. TyrD has a midpoint potential lower than that of TyrZ, and its protein environment is distinguished by potential π-cation interactions with arginine residues. Designed biomimetic peptides provide a system that can be used to investigate how the protein matrix controls PCET reactions. As a model for the redox-active tyrosines in PSII, we are employing a designed, 18 amino acid β hairpin peptide in which PCET reactions occur between a tyrosine (Tyr5) and a cross-strand histidine (His14). In this peptide, the single tyrosine is hydrogen-bonded to an arginine residue, Arg16, and a second arginine, Arg12, has a π-cation interaction with Tyr5. In this report, the effect of these hydrogen bonding and electrostatic interactions on the PCET reactions is investigated. Electrochemical titrations show that histidine substitutions change the nature of PCET reactions, and optical titrations show that Arg16 substitution changes the pK of Tyr5. Removal of Arg16 or Arg12 increases the midpoint potential for tyrosine oxidation. The effects of Arg12 substitution are consistent with the midpoint potential difference, which is observed for the PSII redox-active tyrosine residues. Our results demonstrate that a π-cation interaction, hydrogen bonding, and PCET reactions alter redox-active tyrosine function. These interactions can contribute equally to the control of midpoint potential and reaction rate.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.