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Alternative radical pairs for cryptochrome-based magnetoreception.

Alpha A Lee1, Jason C S Lau, Hannah J Hogben

  • 1Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, , Oxford OX1 3QZ, UK.

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|March 28, 2014
PubMed
Summary
This summary is machine-generated.

A new study suggests a different radical pair, [FAD•- Z•], could be key to avian magnetoreception. This radical pair shows significantly higher sensitivity to Earth's magnetic field than previously assumed [FAD•- TrpH•+].

Keywords:
animal navigationflavinmagnetic compassradical pair mechanismspin dynamics

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Area of Science:

  • Biophysics
  • Quantum Biology
  • Animal Navigation

Background:

  • Avian magnetoreception, the ability of birds to sense Earth's magnetic field, is crucial for navigation.
  • This ability is hypothesized to involve cryptochrome proteins and magnetically sensitive photochemical reactions.
  • The conventional model assumes a [FAD•- TrpH•+] radical pair is involved in magnetoreception.

Purpose of the Study:

  • To investigate the suitability of an alternative radical pair, [FAD•- Z•], as a magnetoreceptor in cryptochrome.
  • To compare the magnetic field sensitivity of [FAD•- Z•] with the conventionally assumed [FAD•- TrpH•+] radical pair.

Main Methods:

  • Quantum spin dynamics simulations were employed to model the reactivity of the [FAD•- Z•] radical pair.
  • The simulations assessed the radical pair's sensitivity to the geomagnetic field under specific conditions (50 µT, 1 µs lifetime).

Main Results:

  • The [FAD•- Z•] radical pair demonstrated a two orders of magnitude greater sensitivity to the geomagnetic field direction compared to [FAD•- TrpH•+].
  • Favorable magnetic properties of [FAD•- Z•] stem from asymmetric hyperfine interactions and optimal flavin radical characteristics.

Conclusions:

  • The [FAD•- Z•] radical pair presents a more sensitive candidate for cryptochrome-based avian magnetoreception.
  • Further research is needed to identify the specific nature of Z• and its formation mechanism within cryptochrome.