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Journal of Biochemistry Advance Access published online on September 28, 2007
Journal of Biochemistry, doi:10.1093/jb/mvm180
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© 2007 The Japanese Biochemical Society

Spectrally- and time-resolved fluorescence spectroscopic study on melittin-calmodulin interaction

Takuhiro Otosu, Etsuko Nishimoto and Shoji Yamashita*

Institute of Biophysics, Faculty of Agriculture, Graduate School of Kyushu University, Hakozaki, Fukuoka 812-8581, Japan

*To whom correspondence should be addressed. Shoji Yamashita: Tel/Fax: +81-92-642-4425. E-mail: yamashita{at}brs.kyushu-u.ac.jp

Received June 28, 2007; Accepted September 6, 2007


  Abstract

The origin of multiexponential fluorescence decay property of tryptophan in protein has been in controversy, and dielectric relaxation is thought to be one of the most plausible candidates of that origin. In this study, we studied melittin-calmodulin interaction on the concept of dielectric relaxation by spectrally- and time-resolved fluorescence spectroscopy. Tryptophan residue in melittin demonstrated drastic change in its dielectric relaxation rate and scale by binding with calmodulin. Expected change of relaxation rate suggested that dielectric relaxation accounts for multiexponential property of fluorescence decay. We also examined the time variation of radiative and nonradiative decay rates. That result demonstrated the distinct difference profiles of nonradiative decay rate of tryptophan in melittin and the complex.

Key Words: calmodulin, dielectric relaxation, melittin, TCSPC, time-resolved fluorescence


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