Search results
Results from the WOW.Com Content Network
The phytol ester of chlorophyll a (R in the diagram) is a long hydrophobic tail which anchors the molecule to other hydrophobic proteins in the thylakoid membrane of the chloroplast. [5] Once detached from the porphyrin ring, phytol becomes the precursor of two biomarkers , pristane and phytane , which are important in the study of geochemistry ...
Due to the presence of chlorophyll a, as opposed to bacteriochlorophyll, Photosystem II absorbs light at a shorter wavelength. The pair of chlorophyll molecules at the reaction center are often referred to as P680. [1] When the photon has been absorbed, the resulting high-energy electron is transferred to a nearby pheophytin molecule.
Photosynthetic reaction centre proteins are main protein components of photosynthetic reaction centres (RCs) of bacteria and plants. They are transmembrane proteins embedded in the chloroplast thylakoid or bacterial cell membrane. Plants, algae, and cyanobacteria have one type of PRC for each of its two photosystems.
Chlorophyll f was announced to be present in cyanobacteria and other oxygenic microorganisms that form stromatolites in 2010; [13] [14] a molecular formula of C 55 H 70 O 6 N 4 Mg and a structure of (2-formyl)-chlorophyll a were deduced based on NMR, optical and mass spectra. [15]
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 ...
Each antenna complex has between 250 and 400 pigment molecules and the energy they absorb is shuttled by resonance energy transfer to a specialized chlorophyll-protein complex known as the reaction center of each photosystem. [1] The reaction center initiates a complex series of chemical reactions that capture energy in the form of chemical bonds.
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 structure of P680 consists of a heterodimer of two distinct chlorophyll molecules, referred to as P D1 and P D2. This “special pair” forms an excitonic dimer that functions as a single unit, excited by light energy as if they were a single molecule.