Alexey Amunts

Structural Analysis of Plant Photosystem I Alexey Amunts

Publisher Marketing: Doctoral Thesis / Dissertation from the year 2010 in the subject Biology - Ecology, grade: -, Tel Aviv University, language: English, comment: The history of Science is nothing else but a Herculean effort of humans to study and resemble the great achievements of Nature. However, despite the recent immense efforts, one of the most hidden secrets of the living world, the one that underpins the survival of virtually all higher-life forms, is still obscure to a large extent. That is the process of photosynthesis. This process is responsible for creation and maintenance of aerobic life on Earth, directly through the generation of oxygen and indirectly through the subsequent biosynthesis of organic compounds that serve as fuel for life., abstract: Photosystem I (PSI) is a multi-subunit and intricate membrane super-complex of protein and non-protein components that catalyzes one of the first steps of oxygenic photosynthesis. PSI captures sunlight through a highly sophisticated pigment network and consequently converts the solar energy into its chemical form providing essential food and fuel to power life on the Earth. PSI operates with the unprecedented quantum efficiency of close to 100%. For this reason, it is regarded as the most efficient light capturing and energy conversion device in Nature. The ability of PSI to convert sunlight energy is highly dependent on the precise spatial arrangement of protein subunits and the relative positions of numerous cofactors. For this reason, we took the challenge of the crystallographic determination of plant PSI structure at a resolution that would allow estimation of single atoms and therefore enable positive identification of most of the amino acid and chlorophyll conformations. We solved the structure of the intact PSI at 3.3 A resolution that revealed exquisitely organized 600 kDa complex of 18 protein subunits, with 46 transmembrane helices and total of 195 cofactors, comprising one of the most complicated membrane protei"