Tracking the Light Environment by Cyanobacteria and the Dynamic Nature of Light Harvesting

Arthur R Grossman,Devaki Bhaya,Qingfang He

doi:10.1074/jbc.r100003200

Arthur R Grossman, Devaki Bhaya + Show 1 more

Open Access

https://doi.org/10.1074/jbc.r100003200

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Abstract

Tracking the Light Environment by Cyanobacteria and the Dynamic Nature of Light Harvesting

Highlights

PBS are peripheral membrane complexes in Cyanobacteria that efficiently harvest light energy and transfer the energy to photosynthetic reaction centers
Phycobiliprotein colors are a consequence of light absorption by linear tetrapyrrole chromophores that covalently associate with the apoproteins [1, 2]
Phycobiliproteins are composed of ␣ and ␤ subunits associated into heterodimers that aggregate into trimers (␣␤)3 and hexamers (␣␤

Summary

Phycobilisome Structure

PBS are peripheral membrane complexes in Cyanobacteria that efficiently harvest light energy and transfer the energy to photosynthetic reaction centers. PBS, which can comprise 30% of the cellular protein, are organized into two structural domains, the core and rods (Fig. 1). Each of these domains contains pigmented and nonpigmented polypeptides. Biliprotein aggregates, and modulate the absorption characteristics of phycobiliproteins, promoting unidirectional energy flow to photosynthetic reaction centers [1]. PBS cores contain AP trimers along with pigmented and L polypeptides. The phycobiliprotein-like domain of LCM binds a tetrapyrrole chromophore and can serve as a PBS terminal energy acceptor. Six rods, each composed of stacks of PC and PE hexamers, radiate from the core, giving PBS a fanlike appearance (Fig. 1) (see Ref. 2 for details)

Complementary Chromatic Adaptation

Findings

Integration of Light and Nutrient Signals in PBS Biosynthesis