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TitleStructure of the antenna complex expressed during far-red light photoacclimation in Synechococcus sp. PCC 7335.
Journal, issue, pagesJ Biol Chem, Vol. 300, Issue 2, Page 105590, Year 2024
Publish dateDec 22, 2023
AuthorsChristopher J Gisriel / Gaozhong Shen / Gary W Brudvig / Donald A Bryant /
PubMed AbstractFar-red light photoacclimation, or FaRLiP, is a facultative response exhibited by some cyanobacteria that allows them to absorb and utilize lower energy light (700-800 nm) than the wavelengths ...Far-red light photoacclimation, or FaRLiP, is a facultative response exhibited by some cyanobacteria that allows them to absorb and utilize lower energy light (700-800 nm) than the wavelengths typically used for oxygenic photosynthesis (400-700 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-EM 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.
External linksJ Biol Chem / PubMed:38141759 / PubMed Central
MethodsEM (single particle)
Resolution2.35 - 2.78 Å
Structure data

42278

8uhe

EMDB-42278, PDB-8uhe:
Structure of the far-red light-absorbing allophycocyanin core expressed during FaRLiP
Method: EM (single particle) / Resolution: 2.78 Å

42281

8uhi

EMDB-42281, PDB-8uhi:
Structure of the far-red light-absorbing allophycocyanin core expressed during FaRLiP
Method: EM (single particle) / Resolution: 2.35 Å

Chemicals

ChemComp-CYC:
PHYCOCYANOBILIN

ChemComp-M1V:
mesobiliverdin IX(alpha)

ChemComp-CL:
Unknown entry

ChemComp-RUB:
RIBULOSE-1,5-DIPHOSPHATE

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • synechococcus sp. pcc 7335 (bacteria)
KeywordsPHOTOSYNTHESIS / light-harvesting / allophycocyanin / phycocyanobilin

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