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The phycobilins are especially efficient at absorbing red, orange, yellow, and green light, wavelengths that are not well absorbed by chlorophyll a. [2] Organisms growing in shallow waters tend to contain phycobilins that can capture yellow/red light, [ 3 ] while those at greater depth often contain more of the phycobilins that can capture ...
Phycocyanobilin is a blue phycobilin, i.e., a tetrapyrrole chromophore found in cyanobacteria and in the chloroplasts of red algae, glaucophytes, and some cryptomonads. Phycocyanobilin is present only in the phycobiliproteins allophycocyanin and phycocyanin, of which it is the terminal acceptor of energy.
Phycoerythrin (PE) is a red protein-pigment complex from the light-harvesting phycobiliprotein family, present in cyanobacteria, [1] red algae [2] and cryptophytes, [3] accessory to the main chlorophyll pigments responsible for photosynthesis.The red pigment is due to the prosthetic group, phycoerythrobilin, which gives phycoerythrin its red color.
Phycocyanin is a characteristic light blue color, absorbing orange and red light, particularly 620 nm (depending on which specific type it is), and emits fluorescence at about 650 nm (also depending on which type it is).
The phycobilins of red algae absorb blue-green light which penetrates deeper into water than red light, enabling them to photosynthesize in deep waters. Each absorbed photon causes the formation of an exciton (an electron excited to a higher energy state) in the pigment molecule.
The spectral property of phycobiliproteins are mainly dictated by their prosthetic groups, which are linear tetrapyrroles known as phycobilins including phycocyanobilin, phycoerythrobilin, phycourobilin and phycobiliviolin. The spectral properties of a given phycobilin are influenced by its protein environment.
Cells need to build, sustain, and sometimes modify their shape, which allows them to rapidly change their behaviour in response to external factors. During different life cycle stages, such as cell growth , cell division or cell differentiation , internal structures must dynamically adapt to the current requirements.
The pigments in photoreceptor proteins either change their conformation or undergo photoreduction when they absorb a photon. [3] This change in the conformation or redox state of the chromophore then affects the protein conformation or activity and triggers a signal transduction cascade. [3] Examples of photoreceptor pigments include: [4]