H2020Индивидуална стипендия2020–2022

OCPSTRUCTDYNAMICS · Structural dynamics essential for photosynthetic adaptation and survival of cyanobacteria in fluctuating light intensities

„Хоризонт 2020“ — Действия „Мария Склодовска-Кюри“

Период
2020-01-08 → 2022-01-07
Финансиране от ЕС
212 934 €
Участници
1
Схема
MSCA-IF

Линиите свързват координатора с партньорите.

Накратко на български

Оранжевият каротеноиден протеин при цианобактериите контролира как тези организми реагират на промени в светлината. Разбирането на този механизъм помага за разработването на устойчиви и екологични технологии за улавяне на слънчева енергия.

Този кратък обзор е генериран от изкуствен интелект

Кратко обяснение, генерирано от езиков модел по текста на CORDIS. Оригиналът е по-долу.

Резултати накратко

Structural dynamics essential for photosynthetic adaptation and survival of cyanobacteria in fluctuating light intensities

Photosynthesis is the primary source of energy in any ecosystem. Solar energy is renewable, non-polluting and available worldwide. Understanding and controlling photosynthetic machinery on a molecular level, in practically in response to environmental changes, is one of the “hot” topics in modern photosynthesis research due to its high potential in green solutions and sustainability. More than half of photosynthesis occurs in the ocean in single-celled organisms. Cyanobacteria are the antient unicellular photosynthesizes which still contribute up to 50% of oxygen and primary product in the ocean. Therefore, they are excellent model organisms with which to study efficient energy harnessing and storage. Orange Carotenoid Protein (OCP) is a key element in cyanobacterial photoprotection against rapid light increases and works as a light harnessing controller. It is also a unique photoreceptor with peculiar structure: it is the only known photosensor which uses carotenoid for its light-activation. In the scope of OCPSTRUCTDYNAMICS the light-activation steps in OCP were addressed.

Текст от CORDIS, на английски · Данни: CORDIS, © Европейски съюз

Цел на проекта

Like most photosynthetic organisms, cyanobacteria are vulnerable to fluctuations in light intensity, which can damage their photosynthetic machinery. To protect themselves against such fluctuations, they use a photoprotective mechanism called non-photochemical quenching (NPQ), i.e. the dissipation of excess absorbed photo-energy as heat. NPQ in cyanobacteria is triggered by orange carotenoid protein (OCP) light activation. Based on spectroscopic and diffraction studies of OCP in Synechocystis 6803 (gene slr1963), it was suggested that OCP light activation occurs through light-induced movement of a carotenoid causing movement and/or dissociation of OCP N- and C-terminal domains. However, the exact structural dynamics of OCP light-activation need to be unravelled. Furthermore, the growing availability of cyanobacterial genomes allowed identification of additional OCP subfamilies (OCP2, OCPX) in different cyanobacteria. The first results demonstrating different kinetics of light-activation in the different OCP paralogs raised questions about differences in their photoprotective roles and in photoactivation mechanisms. This topic has not been studied to date. Here I propose to resolve structural changes during photoprotection-related transitions of OCP in different OCP subfamilies using time-resolved X-ray crystallography. X-ray crystallography of OCP1 encoded by slr1963, the best-characterized OCP protein, as well as its paralogs from the OCP2 and OCPX subfamilies will be performed. This approach will be combined with ultrafast transient (polarised) absorption spectroscopy on isolated proteins and oriented single crystals to describe the structure-dependent flow of photoenergy in the proteins. This study has several potential applications ranging from enhancing cyanobacterial light harvesting to improve biofuel production, to better understanding of carotenoid-protein interactions in artificial photosynthesis systems, and for optogenetics.

Оригинален текст от CORDIS (на английски).

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Данни: CORDIS, © Европейски съюз