Magnetic sensitivity of cryptochrome 4 from a migratory songbird

Xu, Jingjing; Jarocha, Lauren E.; Zollitsch, Tilo; Konowalczyk, Marcin; Henbest, Kevin B.; Richert, Sabine; Golesworthy, Matthew J.; Schmidt, Jessica; Déjean, Victoire; Sowood, Daniel J. C.; Bassetto, Marco; Luo, Jiate; Walton, Jessica R.; Fleming, Jessica L.; Wei, Yujing; Pitcher, Tommy L.; Moise, Gabriel; Herrmann, Maike; Yin, Hang; Wu, Haijia; Bartölke, Rabea; Käsehagen, Stefanie J.; Horst, Simon; Dautaj, Glen; Murton, Patrick D. F.; Gehrckens, Angela S.; Chelliah, Yogarany; Takahashi, Joseph S.; Koch, Karl‐Wilhelm; Weber, Stefan; Solov’yov, Ilia A.; Xie, Can; Mackenzie, Stuart R.; Timmel, Christiane R.; Mouritsen, Henrik; Hore, P. J.

doi:10.1038/s41586-021-03618-9

Cited by 197 publications

(371 citation statements)

References 62 publications

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“…The simulations described below were performed with k relax = 10 6 s −1 (figure 4) and k relax = 10 5 , 10 6 or 10 7 s −1 (figure 5). [39]. All other rate constants, and the free energies of the various states come from molecular dynamics simulations [39].…”

Section: Methodsmentioning

confidence: 99%

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Cryptochrome magnetoreception: four tryptophans could be better than three

Wong

Wei

Mouritsen

et al. 2021

J. R. Soc. Interface.

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The biophysical mechanism of the magnetic compass sensor in migratory songbirds is thought to involve photo-induced radical pairs formed in cryptochrome (Cry) flavoproteins located in photoreceptor cells in the eyes. In Cry4a—the most likely of the six known avian Crys to have a magnetic sensing function—four radical pair states are formed sequentially by the stepwise transfer of an electron along a chain of four tryptophan residues to the photo-excited flavin. In purified Cry4a from the migratory European robin, the third of these flavin–tryptophan radical pairs is more magnetically sensitive than the fourth, consistent with the smaller separation of the radicals in the former. Here, we explore the idea that these two radical pair states of Cry4a could exist in rapid dynamic equilibrium such that the key magnetic and kinetic properties are weighted averages. Spin dynamics simulations suggest that the third radical pair is largely responsible for magnetic sensing while the fourth may be better placed to initiate magnetic signalling particularly if the terminal tryptophan radical can be reduced by a nearby tyrosine. Such an arrangement could have allowed independent optimization of the essential sensing and signalling functions of the protein. It might also rationalize why avian Cry4a has four tryptophans while Crys from plants have only three.

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Section: Methodsmentioning

confidence: 99%

“…[39]. All other rate constants, and the free energies of the various states come from molecular dynamics simulations [39]. FAD* is the photo-excited singlet state of FAD.…”

Section: Methodsmentioning

confidence: 99%

Cryptochrome magnetoreception: four tryptophans could be better than three

Wong

Wei

Mouritsen

et al. 2021

J. R. Soc. Interface.

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“…The combination of laser excitation and electron paramagnetic resonance (EPR) spectroscopy is a powerful approach for the detection of paramagnetic intermediates. Transient or time-resolved EPR (TREPR) [4,14,41] is, therefore, regularly employed in a growing number of laboratories to detect short-lived states including triplets, quintets [35] and radical-pairs [6] in, for example, proteins [43], materials for organic electronics [5,42] or quantum information science [27]. In the field of dipolar spectroscopy and double electron-electron resonance (DEER) photoexcited triplet states offer the possibility of measuring distances in proteins rather than using conventional nitroxide spin-labels (e.g., (2,2,6,6-Tetramethylpiperidin-1-yl)oxyl, TEMPO) [2,3].…”

Section: Introductionmentioning

confidence: 99%

Pentacene in 1,3,5-Tri(1-naphtyl)benzene: A Novel Standard for Transient EPR Spectroscopy at Room Temperature

et al. 2021

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Testing and calibrating an experimental setup with standard samples is an essential aspect of scientific research. Single crystals of pentacene in p-terphenyl are widely used for this purpose in transient electron paramagnetic resonance (EPR) spectroscopy. However, this sample is not without downsides: the crystals need to be grown and the EPR transitions only appear at particular orientations of the crystal with respect to the external magnetic field. An alternative host for pentacene is the glass-forming 1,3,5-tri(1-naphtyl)benzene (TNB). Due to the high glass transition point of TNB, an amorphous glass containing randomly oriented pentacene molecules is obtained at room temperature. Here we demonstrate that pentacene dissolved in TNB gives a typical “powder-like” transient EPR spectrum of the triplet state following pulsed laser excitation. From the two-dimensional data set, it is straightforward to obtain the zero-field splitting parameters and relative populations by spectral simulation as well as the $$B_{1}$$ B 1 field in the microwave resonator. Due to the simplicity of preparation, handling and stability, this system is ideal for adjusting the laser beam with respect to the microwave resonator and for introducing students to transient EPR spectroscopy.

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“…However, the exact mechanism of magnetoreception in animals is still subject to debate, because the corresponding biochemical components linked to the sensory receptors have yet to be identified, isolated, and properly analyzed [11]. Currently, there is another hypothesis for animal sensing the Earth's magnetic field that includes cryptochrome ErCRY4 protein, which has recently been found in the eyes of migratory European robins, and which possesses the right physical properties to be a magnetosensor [12][13][14]. The cryptochrome protein absorbs light and gets photoexcited, meaning that magnetically sensitive intermediates, known as radical pairs, are generated [15].…”

Section: Introductionmentioning

confidence: 99%

“…The cryptochrome protein absorbs light and gets photoexcited, meaning that magnetically sensitive intermediates, known as radical pairs, are generated [15]. Lu et al have recently shown that ErCRY4 protein has the ability to form long-lived radical pairs that have high magnetic sensitivity and can fulfill the physical requirements needed for magnet sensing [12]. In particular, site-specific mutations of ErCRY4 revealed the roles of four flavin-tryptophan radical pairs in generating magnetic-field effects, and in stabilizing potential signaling states in a way that could enable sensing and signaling functions.…”

Section: Introductionmentioning

confidence: 99%

Bioinspired Magnetic Nanochains for Medicine

Kralj

Marchesan

2021

Pharmaceutics

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Superparamagnetic iron oxide nanoparticles (SPIONs) have been widely used for medicine, both in therapy and diagnosis. Their guided assembly into anisotropic structures, such as nanochains, has recently opened new research avenues; for instance, targeted drug delivery. Interestingly, magnetic nanochains do occur in nature, and they are thought to be involved in the navigation and geographic orientation of a variety of animals and bacteria, although many open questions on their formation and functioning remain. In this review, we will analyze what is known about the natural formation of magnetic nanochains, as well as the synthetic protocols to produce them in the laboratory, to conclude with an overview of medical applications and an outlook on future opportunities in this exciting research field.

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Magnetic sensitivity of cryptochrome 4 from a migratory songbird

Cited by 197 publications

References 62 publications

Cryptochrome magnetoreception: four tryptophans could be better than three

Cryptochrome magnetoreception: four tryptophans could be better than three

Pentacene in 1,3,5-Tri(1-naphtyl)benzene: A Novel Standard for Transient EPR Spectroscopy at Room Temperature

Bioinspired Magnetic Nanochains for Medicine

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