Scientists have discovered the structure of one of the important elements of photosynthesis. This discovery could lead to ‘redesigning’ of photosynthesis to obtain a better yield. It could also cater to the immediate need for food security.
Meanwhile, the University of Sheffield, the U.K., conducted this path-breaking research, which could open up a new era in food security. The findings of the research published in Nature, a renowned scientific journal.
Complex Protein Structure Holds Key to the Energy of Living Cells
Additionally, the study divulges the details of the cytochrome b6f structure. It is a protein complex that substantially impacts the growth of the plant through photosynthesis. Photosynthesis refers to the process that produces all oxygen, and food available on this planet. It produces the energy that sustains human civilization and biosphere.
Besides this, making use of a structural model of high resolution, the research team discovered that a protein complex gives the electrical linkage between Photosystems I and II. These are the light-powered chlorophyll-proteins found in the chloroplast of the plant cell. It changes direct sunlight into chemical energy.
Lorna Malone is a PhD student at the University of Sheffield and is a lead author of the study. Consequently, Malone opines that the study offers significant new understanding into how cytochrome b6f makes use of electrical current to power ‘proton battery’. The stored energy can then be utilized to produce adenosine triphosphate (ATP), which supplies energy for processes in living cells. This chemical reaction gives plants all the essential energy needed by plants to convert carbon dioxide into biomass and carbohydrates. Therefore, these substances sustain the food chain on this planet.
Dr Matt Johnson is a reader in the Biochemistry department, the University of Sheffield, and is one of the supervisors of the study. He added that Cytochrome b6f lies at the very core of photosynthesis and it plays a vital role in the regulation of photosynthetic efficiency.
The study carried on in collaboration with the Astbury Centre for Structural Molecular Biology, University of Leeds.