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The oxidised chlorophyll a replaces the electrons by photolysis that involves the oxidation of water molecules to oxygen, protons and electrons. The N-terminus of the chlorophyll a - b binding protein extends into the stroma where it is involved with adhesion of granal membranes and photo-regulated by reversible phosphorylation of its threonine ...
The chlorophyll a/b-binding protein gene, otherwise known as the CAB gene, is one of the most thoroughly characterized clock-regulated genes in plants. [1] There are a variety of CAB proteins that are derived from this gene family. Studies on Arabidopsis plants have shed light on the mechanisms of biological clocks under the regulation of CAB ...
The peridinin-chlorophyll-protein complex (PCP or PerCP) is a soluble molecular complex consisting of the peridinin-chlorophyll a-protein bound to peridinin, chlorophyll, and lipids. The peridinin molecules absorb light in the blue-green wavelengths (470 to 550 nm) and transfer energy to the chlorophyll molecules with extremely high efficiency.
The D1 (PsbA) and D2 (PsbD) photosystem II (PSII) reaction centre proteins from cyanobacteria, algae and plants only show approximately 15% sequence homology with the L and M subunits, however the conserved amino acids correspond to the binding sites of the photochemically active cofactors.
The two modified chlorophyll molecules are early electron acceptors in PSI. They are present one per PsaA/PsaB side, forming two branches electrons can take to reach F x. A 0 accepts electrons from P700*, passes it to A 1 of the same side, which then passes the electron to the quinone on the same side. Different species seems to have different ...
These polypeptides bind to chlorophyll a and β-Carotene and pass the excitation energy on to the reaction centre. [ 1 ] [ 2 ] This family also includes the iron -stress induced chlorophyll-binding protein CP43', encoded by the IsiA gene, which evolved in cyanobacteria from a PSII protein to cope with light limitations and stress conditions.
Chlorophyll was first isolated and named by Joseph Bienaimé Caventou and Pierre Joseph Pelletier in 1817. [7] The presence of magnesium in chlorophyll was discovered in 1906, [8] and was the first detection of that element in living tissue.
The light-dependent version has the accepted name protochlorophyllide reductase.The systematic name is chlorophyllide-a:NADP+ 7,8-oxidoreductase.Other names in common use include NADPH2-protochlorophyllide oxidoreductase, NADPH-protochlorophyllide oxidoreductase, NADPH-protochlorophyllide reductase, protochlorophyllide oxidoreductase, and protochlorophyllide photooxidoreductase.