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Title: Intramolecular photo-switching and intermolecular energy transfer as primary photoevents in photoreceptive processes: The case of Euglena gracilis

Journal Article · · Biochemical and Biophysical Research Communications
;  [1]; ;  [2];  [3]; ;  [2];  [2]
  1. Istituto Sistemi Complessi, CNR, Via Madonna del Piano 10, 50019 Sesto Fiorentino (Italy)
  2. Istituto di Biofisica, CNR, Via Moruzzi 1, 56124 Pisa (Italy)
  3. ISTI, CNR, Via Moruzzi 1, 56124 Pisa (Italy)

In this paper we report the results of measurements performed by FLIM on the photoreceptor of Euglenagracilis. This organelle consists of optically bistable proteins, characterized by two thermally stable isomeric forms: A{sub 498,} non fluorescent and B{sub 462}, fluorescent. Our data indicate that the primary photoevent of Euglena photoreception upon photon absorption consists of two contemporaneous different phenomena: an intramolecular photo-switch (i.e., A{sub 498} becomes B{sub 462}), and a intermolecular and unidirectional Forster-type energy transfer. During the FRET process, the fluorescent B{sub 462} form acts as donor for the non-fluorescent A{sub 498} form of the protein nearby, which acts as acceptor. We hypothesize that in nature these phenomena follow each other with a domino progression along the orderly organized and closely packed proteins in the photoreceptor layer(s), modulating the isomeric composition of the photoreceptive protein pool. This mechanism guarantees that few photons are sufficient to produce a signal detectable by the cell.

OSTI ID:
22199744
Journal Information:
Biochemical and Biophysical Research Communications, Vol. 385, Issue 2; Other Information: Copyright (c) 2009 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
Country of Publication:
United States
Language:
English