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Magnetic Field Effects on B 12 Ethanolamine Ammonia Lyase: Evidence for a Radical Mechanism
Abstract
A change in radical pair recombination rates is one of the few mechanisms by which a magnetic field can interact with a biological system. The kinetic parameter V max /K m (where K m is the Michaelis constant) for the coenzyme B 12 -dependent enzyme ethanolamine ammonia lyase was decreased 25 percent by a static magnetic field near 0.1 tesla (1000 gauss) with unlabeled ethanolamine and decreased 60 percent near 0.15 tesla with perdeuterated ethanolamine. This effect is likely caused by a magnetic field-induced change in intersystem crossing rates between the singlet and triplet spin states in the [cob(II)alamin:5′-deoxyadenosyl radical} spin-correlated radical pair.
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Cited by
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Ritz, T., Adem, S., & Schulten, K. (2000) · Biophysical Journal · doi:10.1016/s0006-3495(00)76629-x · Cited by 1,176
Cryptochromes—a potential magnetoreceptor: what do we know and what do we want to know?
Liedvogel, M., & Mouritsen, H. (2010) · Journal of The Royal Society Interface · doi:10.1098/rsif.2009.0411.focus · Cited by 231
Metadata
- Authors
- Harkins, T. T., & Grissom, C. B.
- Venue
- Science
- Published
- 1994-02-18
- Volume
- 263
- Issue
- 5149
- Pages
- 958-960
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2122485770
- Cited by
- 192
- References
- 0
- FWCI
- 10.45
- Type
- journal article
- Language
- en
- Open access
- closed
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- Harkins, T. T., & Grissom, C. B. (1994). Magnetic Field Effects on B 12 Ethanolamine Ammonia Lyase: Evidence for a Radical Mechanism. Science. https://doi.org/10.1126/science.8310292
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