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    Home > Biochemistry News > Plant Extracts News > Analysis and Reconstitution of Phycobiliproteins: Methods for the Characterization of Bilin Attachment Reactions

    Analysis and Reconstitution of Phycobiliproteins: Methods for the Characterization of Bilin Attachment Reactions

    • Last Update: 2021-03-16
    • Source: Internet
    • Author: User
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    Phycobiliproteins are a homologous family of light-harvesting accessory proteins present in cyanobacteria (
    25
    ,
    51
    ), red algae (
    25
    ), cryptomonads (
    36
    ,
    52
    ), and some species of prochlorophytes (
    41
    ,
    48
    ). The blue, violet, red, or yellow colors of the phycobiliproteins are due to linear tetrapyrrole chromophores called bilins that are covalently attached at cysteine residues (
    25
    ). These water-soluble proteins are composed of α and β subunits. The αβ monomers form (αβ)
    3
    trimers which further stack into (αβ)
    6
    hexamers. These discshaped trimers and hexamers can be stabilized or organized into larger structures by linker proteins. Through the association of several types of phycobiliproteins with these linker proteins [
    69
    ), the large light-harvesting complex called the phycobili-some is formed (
    51
    ,
    63
    ). Cryptomonad phycobiliproteins have a different composition and structural organization and will not be discussed further in this chapter (for reviews on cryptomonad phycobiliproteins, see References
    36
    ,
    52
    ,
    53
    , and
    73
    ).
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