Vibrational spectroscopy explores the photoreaction of LOV domains

Abstract

Plant phototropins (phot) exhibit a peculiar architecture such that two LOV domains (LOV1 and LOV2) are present in a tandem-like arrangement (N-terminal part of the protein), followed by a C-terminal serine/threonine kinase domain that catalyzes the light-driven autophosphorylation of phot ([Huala et al 1997]). The three-dimensional structure of the LOV1 domain from the green algae Chlamydomonas reinhardtii ([Fedorov et al 2003]) and the LOV2 domain from the fern Adiantum capillus-veneris ([Crosson and Moffat 2001], [2002]) have both been determined in the dark state as well as in the corresponding long-lived intermediate state.