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Hauptverfasser: Kish, Monika, Pradhan, Suchitra, Ramsay, Jessica L., Salazar, Paloma Munguía, Phillips, Jonathan, Kattnig, Daniel R.
Format: Preprint
Veröffentlicht: 2026
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Online-Zugang:https://arxiv.org/abs/2604.19579
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author Kish, Monika
Pradhan, Suchitra
Ramsay, Jessica L.
Salazar, Paloma Munguía
Phillips, Jonathan
Kattnig, Daniel R.
author_facet Kish, Monika
Pradhan, Suchitra
Ramsay, Jessica L.
Salazar, Paloma Munguía
Phillips, Jonathan
Kattnig, Daniel R.
contents The light-dependent magnetic compass of night-migratory songbirds is widely hypothesized to rely on the radical pair mechanism within retinal cryptochrome. However, bridging the mechanistic gap between microsecond quantum spin dynamics and the long-lived, global protein conformational changes required for cellular signalling remains a formidable challenge. Here, we apply redox state-resolved hydrogen/deuterium-exchange mass spectrometry (HDX-MS) to map the conformational landscape of European robin cryptochrome 4a (ErCry4a) across its photocycle. We reveal that photochemical reduction drives robust, allosteric structural transitions across key functional nodes, including the phosphate-binding loop (PBL), protrusion loop (PL), FAD-proximal helix α17, and the C-terminal α22/α23 network. Crucially, we isolate the structural fingerprint of the transient semiquinone, the presumed signalling species. Rather than acting as a linear structural stepping-stone, the semiquinone exhibits a distinct, non-monotonic conformational signature characterized by a transient destabilization of the PBL and PL, contrasting sharply with the global rigidification observed in the fully reduced state. These findings establish the semiquinone as a structurally unique and functionally competent biological entity. Our results provide direct biophysical evidence for a dedicated, high-fidelity structural signalling cascade, detailing how localized quantum-level photochemistry is translated into the precise conformational dynamics required for animal navigation.
format Preprint
id arxiv_https___arxiv_org_abs_2604_19579
institution arXiv
publishDate 2026
record_format arxiv
spellingShingle Distinct Structural Dynamics of the Semiquinone State Define a Signalling Pathway in Avian Cryptochrome
Kish, Monika
Pradhan, Suchitra
Ramsay, Jessica L.
Salazar, Paloma Munguía
Phillips, Jonathan
Kattnig, Daniel R.
Biological Physics
Chemical Physics
The light-dependent magnetic compass of night-migratory songbirds is widely hypothesized to rely on the radical pair mechanism within retinal cryptochrome. However, bridging the mechanistic gap between microsecond quantum spin dynamics and the long-lived, global protein conformational changes required for cellular signalling remains a formidable challenge. Here, we apply redox state-resolved hydrogen/deuterium-exchange mass spectrometry (HDX-MS) to map the conformational landscape of European robin cryptochrome 4a (ErCry4a) across its photocycle. We reveal that photochemical reduction drives robust, allosteric structural transitions across key functional nodes, including the phosphate-binding loop (PBL), protrusion loop (PL), FAD-proximal helix α17, and the C-terminal α22/α23 network. Crucially, we isolate the structural fingerprint of the transient semiquinone, the presumed signalling species. Rather than acting as a linear structural stepping-stone, the semiquinone exhibits a distinct, non-monotonic conformational signature characterized by a transient destabilization of the PBL and PL, contrasting sharply with the global rigidification observed in the fully reduced state. These findings establish the semiquinone as a structurally unique and functionally competent biological entity. Our results provide direct biophysical evidence for a dedicated, high-fidelity structural signalling cascade, detailing how localized quantum-level photochemistry is translated into the precise conformational dynamics required for animal navigation.
title Distinct Structural Dynamics of the Semiquinone State Define a Signalling Pathway in Avian Cryptochrome
topic Biological Physics
Chemical Physics
url https://arxiv.org/abs/2604.19579