ArticleProceedings of the National Academy of Sciences of the United States of America2015
Hole hopping through tyrosine/tryptophan chains protects proteins from oxidative damage.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 115 papers.
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115 citing papers in PubMed, 243 citations in OpenAlex.
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- High-yield charge separation along the alternative path in a photosynthetic reaction center: X-ray structure and electrostatic analysis.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Empowering Precision C-H Functionalization: Advances in Peroxygenase Engineering.Angewandte Chemie (International ed. in English) · 2026Review
- Betulin-Amino Acid Molecular Hybrids: Synthesis, Structure and Pharmacological Potential.International journal of molecular sciences · 2026Article
- Structures of variants of Escherichia coli flavodiiron-type nitric oxide reductase reveal changes in the di-iron site.Acta crystallographica. Section D, Structural biology · 2026Article
- From single step hops to emergent biological phenomena.Journal of inorganic biochemistry · 2026Review
- Electron Transport through a Tryptophan Quadruplex in a Dimeric Azurin Construct.The journal of physical chemistry. B · 2026Article
- Oxidizable amino acids around cytochrome P450 hemes.Journal of inorganic biochemistry · 2026Article
- Redox robustness drives LPMO evolution.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Hole migration in cytochrome P450.QRB discovery · 2026Article
- Sortase-mediated ligation of cytochrome c peroxidase and cytochrome c highlights the roles of dynamics and conformational specificity for interprotein electron transfer.Journal of inorganic biochemistry · 2026Article
- Photodynamic Activation of Mammalian and Avian Cholecystokinin Type 1 Receptor Outside of the Pancreatic Acinar Cell Microenvironment.International journal of molecular sciences · 2025Article
- Understanding Anomalous Cage-Escape Dynamics in Photoredox Processes Driven by a Fe(III) N-Heterocyclic Carbene Complex.Journal of the American Chemical Society · 2025Article
- Energetics of tryptophan residues in electron transfer and photoprotection of type-II photosynthetic reaction centers.PNAS nexus · 2025Article
- Structure-Function Analysis of an Understudied Type of LPMO with Unique Redox Properties and Substrate Specificity.ACS catalysis · 2025Article
- Design of Aromatic Interaction Networks in a Protein Cage Modulated by Fluorescent Ligand Binding.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Nickel-Dithiolene Cofactors as Electron Donors and Acceptors in Protein Hosts.The journal of physical chemistry. B · 2025Article
- Electron transfer in biological systems.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Review
- Molecular Insights into the Quenching Mechanism of the Triplet Excited State of Rose Bengal through Oxidative and Reductive Organic Compounds.ACS omega · 2024Article
- Elucidating the Role of OACS environmental Au · 2024Article
55 more citing papers are in PubMed but not listed here.
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2 authors at 1 institution in 1 country.
Funding
Abstract
Living organisms have adapted to atmospheric dioxygen by exploiting its oxidizing power while protecting themselves against toxic side effects. Reactive oxygen and nitrogen species formed during oxidative stress, as well as high-potential reactive intermediates formed during enzymatic catalysis, could rapidly and irreversibly damage polypeptides were protective mechanisms not available. Chains of redox-active tyrosine and tryptophan residues can transport potentially damaging oxidizing equivalents (holes) away from fragile active sites and toward protein surfaces where they can be scavenged by cellular reductants. Precise positioning of these chains is required to provide effective protection without inhibiting normal function. A search of the structural database reveals that about one third of all proteins contain Tyr/Trp chains composed of three or more residues. Although these chains are distributed among all enzyme classes, they appear with greatest frequency in the oxidoreductases and hydrolases. Consistent with a redox-protective role, approximately half of the dioxygen-using oxidoreductases have Tyr/Trp chain lengths ≥3 residues. Among the hydrolases, long Tyr/Trp chains appear almost exclusively in the glycoside hydrolases. These chains likely are important for substrate binding and positioning, but a secondary redox role also is a possibility.
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