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TitleStructure of a dimeric photosystem II complex from a cyanobacterium acclimated to far-red light.
Journal, issue, pagesJ Biol Chem, Vol. 299, Issue 1, Page 102815, Year 2023
Publish dateDec 20, 2022
AuthorsChristopher J Gisriel / Gaozhong Shen / David A Flesher / Vasily Kurashov / John H Golbeck / Gary W Brudvig / Muhamed Amin / Donald A Bryant /
PubMed AbstractPhotosystem II (PSII) is the water-splitting enzyme central to oxygenic photosynthesis. To drive water oxidation, light is harvested by accessory pigments, mostly chlorophyll (Chl) a molecules, which ...Photosystem II (PSII) is the water-splitting enzyme central to oxygenic photosynthesis. To drive water oxidation, light is harvested by accessory pigments, mostly chlorophyll (Chl) a molecules, which absorb visible light (400-700 nm). Some cyanobacteria facultatively acclimate to shaded environments by altering their photosynthetic machinery to additionally absorb far-red light (FRL, 700-800 nm), a process termed far-red light photoacclimation or FaRLiP. During far-red light photoacclimation, FRL-PSII is assembled with FRL-specific isoforms of the subunits PsbA, PsbB, PsbC, PsbD, and PsbH, and some Chl-binding sites contain Chls d or f instead of the usual Chl a. The structure of an apo-FRL-PSII monomer lacking the FRL-specific PsbH subunit has previously been determined, but visualization of the dimeric complex has remained elusive. Here, we report the cryo-EM structure of a dimeric FRL-PSII complex. The site assignments for Chls d and f are consistent with those assigned in the previous apo-FRL-PSII monomeric structure. All sites that bind Chl d or Chl f at high occupancy exhibit a FRL-specific interaction of the formyl moiety of the Chl d or Chl f with the protein environment, which in some cases involves a phenylalanine sidechain. The structure retains the FRL-specific PsbH2 subunit, which appears to alter the energetic landscape of FRL-PSII, redirecting energy transfer from the phycobiliprotein complex to a Chl f molecule bound by PsbB2 that acts as a bridge for energy transfer to the electron transfer chain. Collectively, these observations extend our previous understanding of the structure-function relationship that allows PSII to function using lower energy FRL.
External linksJ Biol Chem / PubMed:36549647 / PubMed Central
MethodsEM (single particle)
Resolution2.6 Å
Structure data

28539

8eqm

EMDB-28539, PDB-8eqm:
Structure of a dimeric photosystem II complex acclimated to far-red light
Method: EM (single particle) / Resolution: 2.6 Å

Chemicals

ChemComp-OEX:
CA-MN4-O5 CLUSTER

ChemComp-FE2:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-CLA:
CHLOROPHYLL A

ChemComp-PHO:
PHEOPHYTIN A

ChemComp-BCR:
BETA-CAROTENE

ChemComp-SQD:
1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL

ChemComp-PL9:
2,3-DIMETHYL-5-(3,7,11,15,19,23,27,31,35-NONAMETHYL-2,6,10,14,18,22,26,30,34-HEXATRIACONTANONAENYL-2,5-CYCLOHEXADIENE-1,4-DIONE-2,3-DIMETHYL-5-SOLANESYL-1,4-BENZOQUINONE

ChemComp-BCT:
BICARBONATE ION / pH buffer*YM

ChemComp-LHG:
1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE / phospholipid*YM


ChemComp, No image

ChemComp-F6C:
Chlorophyll F

ChemComp-DGD:
DIGALACTOSYL DIACYL GLYCEROL (DGDG)

ChemComp-CL7:
CHLOROPHYLL D

ChemComp-LMG:
1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-RRX:
(3R)-beta,beta-caroten-3-ol

ChemComp-LMT:
DODECYL-BETA-D-MALTOSIDE / detergent*YM

ChemComp-HOH:
WATER

Source
  • synechococcus sp. pcc 7335 (bacteria)
KeywordsPHOTOSYNTHESIS / Far-red / photosystem II / cyanobacteria / chlorophyll

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