ArticleACS omega2023
Mutational Study of the Tryptophan Tetrad Important for Electron Transfer in European Robin Cryptochrome 4a.
Article in ACS omega, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed.
- A Charge-Reversal Point Mutation Completely Depletes Flavin Chromophore from European Robin Cryptochrome 4a Protein.The journal of physical chemistry letters · 2026Article
- Protein and Solvent Reorganization Drives Radical Pair Stability in Avian Cryptochrome 4a.Journal of the American Chemical Society · 2025Article
- Cryptochrome magnetoreception: Time course of photoactivation from non-equilibrium coarse-grained molecular dynamics.Computational and structural biotechnology journal · 2024Article
- Understanding the Red Shift in the Absorption Spectrum of the FAD Cofactor in ClCry4 Protein.The journal of physical chemistry. B · 2024Article
- Magnetic orientation in juvenile Atlantic herring (Journal of the Royal Society, Interface · 2024Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ability of migratory birds to sense magnetic fields has been known for decades, although the understanding of the underlying mechanism is still elusive. Currently, the strongest magnetoreceptor candidate in birds is a protein called cryptochrome 4a. The cryptochrome 4a protein has changed through evolution, apparently endowing some birds with a more pronounced magnetic sensitivity than others. Using phylogenetic tools, we show that a specific tryptophan tetrad and a tyrosine residue predicted to be essential for cryptochrome activation are highly conserved in the avian clade. Through state-of-the-art molecular dynamics simulations and associated analyses, we also studied the role of these specific residues and the associated mutants on the overall dynamics of the protein. The analyses of the single residue mutations were used to judge how far a local change in the protein structure can impact specific dynamics of European robin cryptochrome 4a. We conclude that the replacements of each of the tryptophans one by one with a phenylalanine do not compromise the overall stability of the protein.
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Registered trials
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