Avian cryptochrome 4 binds superoxide

Deviers, Jean; Cailliez, Fabien; de la Lande, Aurélien; Kattnig, Daniel R.

doi:10.1016/j.csbj.2023.12.009

Cited by 2 publications

(1 citation statement)

References 72 publications

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“…The singlet and triplet states of this RP can be converted into the FADH • state through additional FAD •+ protonation, leading to Cry4 entering the signaling state. This FADH • state is either further reduced or results in another radical pair [FADH • O 2 •– ] that was speculated to be magnetic field sensitive. − In this study, the FAD cofactor is considered to be in the FADH • state.…”

Section: Introductionmentioning

confidence: 99%

Understanding the Red Shift in the Absorption Spectrum of the FAD Cofactor in ClCry4 Protein

Kretschmer,

Frederiksen,

Reinholdt

et al. 2024

J. Phys. Chem. B

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It is still a puzzle that has not been entirely solved how migratory birds utilize the Earth's magnetic field for biannual migration. The most consistent explanation thus far is rooted in the modulation of the biological function of the cryptochrome 4 (Cry4) protein by an external magnetic field. This phenomenon is closely linked with the flavin adenine dinucleotide (FAD) cofactor that is noncovalently bound in the protein. Cry4 is activated by blue light, which is absorbed by the FAD cofactor. Subsequent electron and proton transfers trigger radical pair formation in the protein, which is sensitive to the external magnetic field. An important long-lasting redox state of the FAD cofactor is the signaling (FADH • ) state, which is present after the transient electron transfer steps have been completed. Recent experimental efforts succeeded in crystallizing the Cry4 protein from Columbia livia (ClCry4) with all of the important residues needed for protein photoreduction. This specific crystallization of Cry4 protein so far is the only avian cryptochrome crystal structure available, which, however, has great similarity to the Cry4 proteins of night migratory birds. The previous experimental studies of the ClCry4 protein included the absorption properties of the protein in its different redox states. The absorption spectrum of the FADH • state demonstrated a peculiar red shift compared to the photoabsorption properties of the FAD cofactor in its FADH • state in other Cry proteins from other species. The aim of this study is to understand this red shift by employing the tools of computational microscopy and, in particular, a QM/MM approach that relies on the polarizable embedding approximation.

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Section: Introductionmentioning

confidence: 99%

Understanding the Red Shift in the Absorption Spectrum of the FAD Cofactor in ClCry4 Protein

Kretschmer,

Frederiksen,

Reinholdt

et al. 2024

J. Phys. Chem. B

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A structural decryption of cryptochromes

DeOliveira,

Crane

2024

Front. Chem.

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Cryptochromes (CRYs), which are signaling proteins related to DNA photolyases, play pivotal roles in sensory responses throughout biology, including growth and development, metabolic regulation, circadian rhythm entrainment and geomagnetic field sensing. This review explores the evolutionary relationships and functional diversity of cryptochromes from the perspective of their molecular structures. In general, CRY biological activities derive from their core structural architecture, which is based on a Photolyase Homology Region (PHR) and a more variable and functionally specific Cryptochrome C-terminal Extension (CCE). The α/β and α-helical domains within the PHR bind FAD, modulate redox reactive residues, accommodate antenna cofactors, recognize small molecules and provide conformationally responsive interaction surfaces for a range of partners. CCEs add structural complexity and divergence, and in doing so, influence photoreceptor reactivity and tailor function. Primary and secondary pockets within the PHR bind myriad moieties and collaborate with the CCEs to tune recognition properties and propagate chemical changes to downstream partners. For some CRYs, changes in homo and hetero-oligomerization couple to light-induced conformational changes, for others, changes in posttranslational modifications couple to cascades of protein interactions with partners and effectors. The structural exploration of cryptochromes underscores how a broad family of signaling proteins with close relationship to light-dependent enzymes achieves a wide range of activities through conservation of key structural and chemical properties upon which function-specific features are elaborated.

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Avian cryptochrome 4 binds superoxide

Cited by 2 publications

References 72 publications

Understanding the Red Shift in the Absorption Spectrum of the FAD Cofactor in ClCry4 Protein

Understanding the Red Shift in the Absorption Spectrum of the FAD Cofactor in ClCry4 Protein

A structural decryption of cryptochromes

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