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TitleMolecular basis of plastoquinone reduction in plant cytochrome bf.
Journal, issue, pagesNat Plants, Vol. 10, Issue 11, Page 1814-1825, Year 2024
Publish dateOct 3, 2024
AuthorsSebastian Pintscher / Rafał Pietras / Bohun Mielecki / Mateusz Szwalec / Anna Wójcik-Augustyn / Paulina Indyka / Michał Rawski / Łukasz Koziej / Marcin Jaciuk / Grzegorz Ważny / Sebastian Glatt / Artur Osyczka /
PubMed AbstractA multi-subunit enzyme, cytochrome bf (cytbf), provides the crucial link between photosystems I and II in the photosynthetic membranes of higher plants, transferring electrons between plastoquinone ...A multi-subunit enzyme, cytochrome bf (cytbf), provides the crucial link between photosystems I and II in the photosynthetic membranes of higher plants, transferring electrons between plastoquinone (PQ) and plastocyanin. The atomic structure of cytbf is known, but its detailed catalytic mechanism remains elusive. Here we present cryogenic electron microscopy structures of spinach cytbf at 1.9 Å and 2.2 Å resolution, revealing an unexpected orientation of the substrate PQ in the haem ligand niche that forms the PQ reduction site (Q). PQ, unlike Q inhibitors, is not in direct contact with the haem. Instead, a water molecule is coordinated by one of the carbonyl groups of PQ and can act as the immediate proton donor for PQ. In addition, we identify water channels that connect Q with the aqueous exterior of the enzyme, suggesting that the binding of PQ in Q displaces water through these channels. The structures confirm large movements of the head domain of the iron-sulfur protein (ISP-HD) towards and away from the plastoquinol oxidation site (Q) and define the unique position of ISP-HD when a Q inhibitor (2,5-dibromo-3-methyl-6-isopropylbenzoquinone) is bound. This work identifies key conformational states of cytbf, highlights fundamental differences between substrates and inhibitors and proposes a quinone-water exchange mechanism.
External linksNat Plants / PubMed:39362993 / PubMed Central
MethodsEM (single particle)
Resolution1.94 - 2.33 Å
Structure data

19938

9es7

EMDB-19938, PDB-9es7:
Cryo-EM structure of Spinacia oleracea cytochrome b6f complex with water molecules at 1.94 A resolution
Method: EM (single particle) / Resolution: 1.94 Å

19939

9es8

EMDB-19939, PDB-9es8:
Cryo-EM structure of Spinacia oleracea cytochrome b6f with decylplastoquinone bound at plastoquionol reduction site
Method: EM (single particle) / Resolution: 2.24 Å

19940

9es9

EMDB-19940, PDB-9es9:
Cryo-EM structure of Spinacia oleracea cytochrome b6f complex with inhibitor DBMIB bound at plastoquinol oxidation site
Method: EM (single particle) / Resolution: 2.33 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-HEC:
HEME C

ChemComp-UMQ:
UNDECYL-MALTOSIDE / detergent*YM

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

ChemComp-CLA:
CHLOROPHYLL A

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

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

ChemComp-BCR:
BETA-CAROTENE

ChemComp-HOH:
WATER

PDB-1h65:
Crystal structure of pea Toc34 - a novel GTPase of the chloroplast protein translocon

ChemComp-BNT:
2,5-DIBROMO-3-ISOPROPYL-6-METHYLBENZO-1,4-QUINONE

Source
  • spinacia oleracea (spinach)
KeywordsOXIDOREDUCTASE / b6f complex / photosynthesis / membrane protein / electron transport / proton transport / quinone catalysis / water channels / inhibitor

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