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Journal of Biochemistry Advance Access originally published online on September 28, 2007
Journal of Biochemistry 2007 142(5):655-661; 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. 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 multi-exponential fluorescence decay property of tryptophan (Trp) 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. Trp 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 multi-exponential property of fluorescence decay. We also examined the time variation of radiative and non-radiative decay rates. That result demonstrated the distinct difference profiles of non-radiative decay rate of Trp in melittin and the complex.

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

Abbreviations: CaM, calmodulin; EDTA, ethylenediaminetetraacetic acid; FWHM, full width at half-maximum; NATA, N-acetyl-l-tryptophanamide; TCA, trichloroacetic acid; TCSPC, time-correlated single photon counting


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