Abstract
Luminous organisms use different protein-mediated strategies to modulate light emission color. Here, we report the transient-state kinetic studies of the interaction between photoprotein clytin from Clytia gregaria and its antenna protein, cgreGFP. We propose that cgreGFP forms a transient complex with Ca2+-bound clytin before the excited singlet state of the coelenteramide product is formed. From the spectral distribution and donor-acceptor separation distance, we infer that clytin reaction intermediates may interact only with the middle side part of cgreGFP.
Original language | English |
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Pages (from-to) | 307-316 |
Journal | FEBS Letters |
Volume | 590 |
Issue number | 3 |
DOIs | |
Publication status | Published - 2016 |
Keywords
- aequorin
- bioluminescence
- coelenterazine
- FRET
- obelin
- protein-protein interaction