ArticleThe journal of physical chemistry letters2026
A Charge-Reversal Point Mutation Completely Depletes Flavin Chromophore from European Robin Cryptochrome 4a Protein.
Article in The journal of physical chemistry letters, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed.
- Protein-Solvent Interface Controls Proton-Coupled Reactivity in Cryptochrome 4a.Journal of the American Chemical Society · 2026Article
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7 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Cryptochrome 4a (Cry4a) is a magnetically sensitive protein that could enable night-migratory birds to sense the geomagnetic field for navigation. The key to the protein's magnetic sensitivity is the flavin adenine dinucleotide (FAD) cofactor, which initiates the electron transfer within the protein, leading to a spin-correlated radical pair. Despite its importance, the mechanism of FAD binding in avian Cry4a proteins remains unclear. Here, we show that a point mutation of the positively charged arginine residue at position 356 to a negatively charged glutamic acid (R356E) completely depletes FAD binding from European robin (
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