Global diffusion and solution structure of photo-switchable proteins from cyanobacteria
In cyanobacteria, photosynthesis is initiated by light-absorption in protein complexes referred to as phycobilisomes. In the presence of excess light, photodamage is prevented by so called non-photochemical quenching (NPQ). This regulative process is realized by the interplay between the light harvesting phycobilisomes and a light-sensitive effector of NPQ referred to as the Orange Carotenoid Protein (OCP). OCP has to undergo a light-induced structural change from its inactive orange state OCPO to an active red state OCPR, which can be initiated by illumination using a laser wavelength of 450 nm at 300 K. It is important to emphasize that the rate of NPQ is limited by the diffusion of the water-soluble OCPs towards the membrane-extrinsic phycobilisomes so that an accurate determination of the diffusion constants is pivotal for a quantitative understanding of NPQ. Here, we propose to study the global diffusion in the inactive orange state OCPO, in the active red state OCPR induced by in-situ illumination, and using a mutant assumed to mimic the active state in the dark. Complementary SEC-SANS experiments using D22 are meant to establish the respective solution structures.
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MOLDENHAUER Marcus; APPEL Markus; GOLUB Maksym; Mina Hajizadeh omaslanolya; MATSARSKAIA Olga; PIEPER Joerg; PORCAR Lionel and SEYDEL Tilo. (2021). Global diffusion and solution structure of photo-switchable proteins from cyanobacteria. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-924
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