Structural highlights
Function
B4WNZ8_SYNS7 RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. Although the small subunit is not catalytic it is essential for maximal activity.[HAMAP-Rule:MF_00859]
Publication Abstract from PubMed
Far-red light photoacclimation, or FaRLiP, is a facultative response exhibited by some cyanobacteria that allows them to absorb and utilize lower energy light (700 to 800 nm) than the wavelengths typically used for oxygenic photosynthesis (400 to 700 nm). During this process, three essential components of the photosynthetic apparatus are altered: photosystem I, photosystem II, and the phycobilisome. In all three cases, at least some of the chromophores found in these pigment-protein complexes are replaced by chromophores that have red-shifted absorbance relative to the analogous complexes produced in visible light. Recent structural and spectroscopic studies have elucidated important features of the two photosystems when altered to absorb and utilize far-red light, but much less is understood about the modified phycobiliproteins made during FaRLiP. We used single-particle, cryo-electron microscopy to determine the molecular structure of a phycobiliprotein core complex comprising allophycocyanin variants that absorb far-red light during FaRLiP in the marine cyanobacterium Synechococcus sp. PCC 7335. The structure reveals the arrangement of the numerous red-shifted allophycocyanin variants and the probable locations of the chromophores that serve as the terminal emitters in this complex. It also suggests how energy is transferred to the photosystem II complexes produced during FaRLiP. The structure additionally allows comparisons with other previously studied allophycocyanins to gain insights into how phycocyanobilin chromophores can be tuned to absorb far-red light. These studies provide new insights into how far-red light is harvested and utilized during FaRLiP, a widespread cyanobacterial photoacclimation mechanism.
Structure of the antenna complex expressed during far-red light photoacclimation in Synechococcus sp. PCC 7335.,Gisriel CJ, Shen G, Brudvig GW, Bryant DA J Biol Chem. 2023 Dec 21:105590. doi: 10.1016/j.jbc.2023.105590. PMID:38141759[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gisriel CJ, Shen G, Brudvig GW, Bryant DA. Structure of the antenna complex expressed during far-red light photoacclimation in Synechococcus sp. PCC 7335. J Biol Chem. 2023 Dec 21:105590. PMID:38141759 doi:10.1016/j.jbc.2023.105590
