THE CHLOROPHYLL-CAROTENOID PROTEINS OF OXYGENIC PHOTOSYNTHESIS

Plants cells contain a number of structures that are involved in the process of photosynthesis:

Photosynthesis | Biology | Science | Khan Academy

Human caused increases in atmospheric CO2 are predicted to double the CO2 by the middle to end of the next century (from 360 to 720 ppm CO2). Based on your results above, what do expect to happen to photosynthesis ?

Diagram of a plant cell involved in production of glucose from photosynthesis

Glossary of Terms: P - Physical Geography

Meat-eating plants do not eat for energy; they eat to obtain nutrients, such as nitrogen and phosphate, to build the proteins needed for photosynthesis.

Living organisms besides plants do photosynthesis.

Nucleus - containing DNA carrying the genetic code for enzymes and other proteins used in photosynthesis

This process is called photomorphogenesis.

Weed killers called herbicides work by targeting enzymes used in the light reactions of photosynthesis.

In photosynthetic bacteria, the proteins that gather light for photosynthesis are embedded in cell membranes


IB Biology Notes - 7.5 Proteins

-Phosphorylation has been shown in photosynthesis-related proteins in a cyanobacterium sp. strain PCC 6803 (thereafter 6803), suggesting that phosphorylation of S, T, and Y residues might be important in photosynthesis-related processes. Investigation of biological roles of these phosphorylation events requires confident knowledge of the phosphorylated sites and prospects for their individual assessment. We performed phosphoproteomic analysis of 6803 using TiO2 enrichment of the phosphopeptides, followed by LC–MS/MS, and discovered 367 phosphorylation sites in 190 proteins participating in various cellular functions. Furthermore, we focused on the large group of phosphoproteins that are involved in light harvesting, photosynthesis-driven electron flow, photoprotection, and CO2 fixation. The SRM approach was applied to verify/improve assignments of phosphorylation sites in these proteins and to investigate possibilities for analysis of phosphopeptide isomers. The SRM assays were designed for peptides comprising 45 phosphorylation sites. The assays contain peptide iRT values and Q1/Q3 transitions comprising those discriminating between phosphopeptide isoforms. The majority of investigated phosphopeptides and phosphorylated isoforms could be individually assessed with the SRM technique. The assays could be potentially used in future quantitative studies to evaluate an extent of phosphorylation in photosynthesis-related proteins in 6803 cells challenged with various environmental stresses.