Phycoerythrobilin

About: Phycoerythrobilin is a research topic. Over the lifetime, 212 publications have been published within this topic receiving 7891 citations.

Phycobilisome and Phycobiliprotein Structures

Abstract: Phycobilisomes serve as the primary light-harvesting antennae for Photosystem II in cyanobacteria and red algae. These supramolecular complexes are primarily composed of phycobiliproteins, a brilliantly colored family of water-soluble proteins bearing covalently attached, open-chain tetrapyrroles known as phycobilins. In addition, phycobilisomes also contain smaller amounts ‘linker polypeptides,’ most of which do not bear chromophores. These components are absolutely required for proper assembly and functional organization of the structure. Phycobilisomes are constructed from two main structural elements: a core substructure and peripheral rods that are arranged in a hemidiscoidal fashion around that core. The core of most hemidiscoidal phycobilisomes is composed of three cylindrical subassemblies. The peripheral rods radiate from the lateral surfaces of the core substructure which are not in contact with the thylakoid membrane. Absorbed light energy is transferred by very rapid, radiation-less downhill energy transfer from phycoerythrin or phycoerythrocyanin (if present) to C-phycocyanin and then to allophycocyanin species that act as the final energy transmitters from the phycobilisome to the Photosystem II or (partially) Photosystem I reaction centers.

Functional Genomic Analysis of the HY2 Family of Ferredoxin-Dependent Bilin Reductases from Oxygenic Photosynthetic Organisms

Abstract: Phytobilins are linear tetrapyrrole precursors of the light-harvesting prosthetic groups of the phytochrome photoreceptors of plants and the phycobiliprotein photosynthetic antennae of cyanobacteria, red algae, and cryptomonads. Previous biochemical studies have established that phytobilins are synthesized from heme via the intermediacy of biliverdin IXα (BV), which is reduced subsequently by ferredoxin-dependent bilin reductases with different double-bond specificities. By exploiting the sequence of phytochromobilin synthase (HY2) of Arabidopsis, an enzyme that catalyzes the ferredoxin-dependent conversion of BV to the phytochrome chromophore precursor phytochromobilin, genes encoding putative bilin reductases were identified in the genomes of various cyanobacteria, oxyphotobacteria, and plants. Phylogenetic analyses resolved four classes of HY2-related genes, one of which encodes red chlorophyll catabolite reductases, which are bilin reductases involved in chlorophyll catabolism in plants. To test the catalytic activities of these putative enzymes, representative HY2-related genes from each class were amplified by the polymerase chain reaction and expressed in Escherichia coli. Using a coupled apophytochrome assembly assay and HPLC analysis, we examined the ability of the recombinant proteins to catalyze the ferredoxin-dependent reduction of BV to phytobilins. These investigations defined three new classes of bilin reductases with distinct substrate/product specificities that are involved in the biosynthesis of the phycobiliprotein chromophore precursors phycoerythrobilin and phycocyanobilin. Implications of these results are discussed with regard to the pathways of phytobilin biosynthesis and their evolution.

Chromatic adaptation in marine Synechococcus strains.

Abstract: Characterization of two genetically distinct groups of marine Synechococcus sp. strains shows that one, but not the other, increases its phycourobilin/phycoerythrobilin chromophore ratio when growing in blue light. This ability of at least some marine Synechococcus strains to chromatically adapt may help explain their greater abundance in particular ocean environments than cyanobacteria of the genus Prochlorococcus.