AI Article Synopsis
- Cyanobacteria utilize phycobilisomes (PBSs) to efficiently capture light energy, which are organized near chlorophyll-containing reaction centers for optimal energy conversion.
- PBSs consist of stacked phycobiliproteins (PBPs) and linker proteins, with the PBPs structured as heterodimers made up of distinct alpha and beta polypeptides, each featuring seven alpha-helices.
- The review aims to summarize recent advancements in understanding PBSs and PBPs, while also addressing unresolved questions in the field of light-dependent processes in cyanobacteria.
Article Abstract
Cyanobacteria trap light energy by arrays of pigment molecules termed "phycobilisomes (PBSs)", organized proximal to "reaction centers" at which chlorophyll perform the energy transduction steps with highest quantum efficiency. PBSs, composed of sequential assembly of various chromophorylated phycobiliproteins (PBPs), as well as nonchromophoric, basic and hydrophobic polypeptides called linkers. Atomic resolution structure of PBP is a heterodimer of two structurally related polypeptides but distinct specialised polypeptides- a and ß, made up of seven alpha-helices each which played a crucial step in evolution of PBPs. PBPs carry out various light dependent responses such as complementary chromatic adaptation. The aim of this review is to summarize and discuss the recent progress in this field and to highlight the new and the questions that remain unresolved.
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|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4553884 | PMC |
| http://dx.doi.org/10.17179/excli2014-723 | DOI Listing |
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