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TitleDe novo design of proteins housing excitonically coupled chlorophyll special pairs.
Journal, issue, pagesNat Chem Biol, Vol. 20, Issue 7, Page 906-915, Year 2024
Publish dateJun 3, 2024
AuthorsNathan M Ennist / Shunzhi Wang / Madison A Kennedy / Mariano Curti / George A Sutherland / Cvetelin Vasilev / Rachel L Redler / Valentin Maffeis / Saeed Shareef / Anthony V Sica / Ash Sueh Hua / Arundhati P Deshmukh / Adam P Moyer / Derrick R Hicks / Avi Z Swartz / Ralph A Cacho / Nathan Novy / Asim K Bera / Alex Kang / Banumathi Sankaran / Matthew P Johnson / Amala Phadkule / Mike Reppert / Damian Ekiert / Gira Bhabha / Lance Stewart / Justin R Caram / Barry L Stoddard / Elisabet Romero / C Neil Hunter / David Baker /
PubMed AbstractNatural photosystems couple light harvesting to charge separation using a 'special pair' of chlorophyll molecules that accepts excitation energy from the antenna and initiates an electron-transfer ...Natural photosystems couple light harvesting to charge separation using a 'special pair' of chlorophyll molecules that accepts excitation energy from the antenna and initiates an electron-transfer cascade. To investigate the photophysics of special pairs independently of the complexities of native photosynthetic proteins, and as a first step toward creating synthetic photosystems for new energy conversion technologies, we designed C-symmetric proteins that hold two chlorophyll molecules in closely juxtaposed arrangements. X-ray crystallography confirmed that one designed protein binds two chlorophylls in the same orientation as native special pairs, whereas a second designed protein positions them in a previously unseen geometry. Spectroscopy revealed that the chlorophylls are excitonically coupled, and fluorescence lifetime imaging demonstrated energy transfer. The cryo-electron microscopy structure of a designed 24-chlorophyll octahedral nanocage with a special pair on each edge closely matched the design model. The results suggest that the de novo design of artificial photosynthetic systems is within reach of current computational methods.
External linksNat Chem Biol / PubMed:38831036 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2 - 6.5 Å
Structure data

40208

8glt

EMDB-40208, PDB-8glt:
Backbone model of de novo-designed chlorophyll-binding nanocage O32-15
Method: EM (single particle) / Resolution: 6.5 Å

EMDB-40209: Chlorophyll-binding region of de novo-designed nanocage O32-15
Method: EM (single particle) / Resolution: 5.2 Å

PDB-7unh:
De novo designed chlorophyll dimer protein in apo state, SP2
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-7uni:
De novo designed chlorophyll dimer protein with Zn pheophorbide a methyl ester, SP2-ZnPPaM
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-7unj:
De novo designed chlorophyll dimer protein with Zn pheophorbide a methyl ester matching geometry of purple bacterial special pair, SP1-ZnPPaM
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-8evm:
De novo design of chlorophyll special pair containing protein assemblies
Method: X-RAY DIFFRACTION / Resolution: 3.05 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-OE9:
[methyl 9-ethenyl-14-ethyl-3-(3-methoxy-3-oxopropyl)-4,8,13,18-tetramethyl-20-oxophorbine-21-carboxylatato(2-)-kappa~4~N~23~,N~24~,N~25~,N~26~]zinc

ChemComp-PO4:
PHOSPHATE ION

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-SO4:
SULFATE ION

Source
  • synthetic construct (others)
KeywordsDE NOVO PROTEIN / design / homodimer / rosetta / symmetric / designed / circular tandem repeat protein / cTRP / apo / chlorophyll / Zn pheophorbide a methyl ester / Zn / de novo design / electron donor / photosynthetic / nanocage / helical repeats / chlorophyll-binding / octahedral symmetry

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