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Chlorophyll b is a form of chlorophyll. Chlorophyll b helps in photosynthesis by absorbing light energy. It is more soluble than chlorophyll a in polar solvents because of its carbonyl group. Its color is green, and it primarily absorbs blue light. [2] In land plants, the light-harvesting antennae around photosystem II contain the majority of ...
Chlorophyll b is made by the same enzyme acting on chlorophyllide b. The same is known for chlorophyll d and f, both made from corresponding chlorophyllides ultimately made from chlorophyllide a. [39] In Angiosperm plants, the later steps in the biosynthetic pathway are light-dependent. Such plants are pale if grown in darkness.
The light-harvesting complex (or antenna complex; LH or LHC) is an array of protein and chlorophyll molecules embedded in the thylakoid membrane of plants and cyanobacteria, which transfer light energy to one chlorophyll a molecule at the reaction center of a photosystem. The antenna pigments are predominantly chlorophyll b, xanthophylls, and ...
At the reaction center, there are many polypeptides that are surrounded by pigment proteins. At the center of the reaction center is a special pair of chlorophyll molecules. Each PSII has about 8 LHCII. These contain about 14 chlorophyll a and chlorophyll b molecules, as well as about four carotenoids. In the reaction center of PSII of plants ...
Chlorophyll b: a yellow-green pigment; Chlorophyll a is the most common of the six, present in every plant that performs photosynthesis. Each pigment absorbs light more efficiently in a different part of the electromagnetic spectrum. Chlorophyll a absorbs well in the ranges of 400–450 nm and at 650–700 nm; chlorophyll b at 450–500 nm and ...
BChl roughly resembles the chlorophyll molecule found in green plants, but, due to minor structural differences, its peak absorption wavelength is shifted into the infrared, with wavelengths as long as 1000 nm. Bph has the same structure as BChl, but the central magnesium ion is replaced by two protons.
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Liu et al. (2004) Crystal structure of spinach major light-harvesting complex at 2.72A° resolution. Nature 428: 287–292. Lokstein (1994)The role of light-harvesting complex II energy dissipation: an in-vivo fluorescence in excess excitation study on the origin of high-energy quenching. Journal of Photochemistry and Photobiology 26: 175-184