We are
currently investigating a recently discovered blue-light photoreceptor
cryptochrome, a sequence analogue of photolyase, but having a
totally different function. This flavoprotein uses photon energy to
synchronize the circadian clock. We are characterizing initial
signaling-state formation and transduction in these complexes with
state-of-the-art femtosecond spectroscopy. Dynamics and function are
well synchronized by femtosecond pulse initiation and their temporal
evolution will be directly probed. Complex recognition and
conformational changes will be studied at longer time scales. Abnormal
clock function causes a variety of diseases and syndromes and these
studies will reveal molecular mechanisms of biological timing.
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Ultrafast dynamics and anionic active states of the flavin cofactor in cryptochrome and photolyase.
Y.-T. Kao, C. Tan, S.-H. Song, N. Ozturk, J. Li, L. Wang, A. Sancar and D. Zhong, J. Am. Chem. Soc. 130, 7695 (2008).
[Web link]
[PDF]
Ultrafast dynamics of flavins in five redox states.
Y.-T. Kao, C. Saxena, T.-F. He, L. Guo, L. Wang, A. Sancar and D. Zhong, J. Am. Chem. Soc. 130, 13132 (2008).
[Web link]
[PDF]
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