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5VJT

De Novo Photosynthetic Reaction Center Protein Equipped with Heme B and Zn(II) cations

Summary for 5VJT
Entry DOI10.2210/pdb5vjt/pdb
Related5VJS 5VJU
DescriptorReaction Center Maquette, ZINC ION, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total)
Functional Keywordsmaquette, protein design, charge separation, artificial photosynthesis, de novo protein
Biological sourcesynthetic construct
Total number of polymer chains1
Total formula weight23384.09
Authors
Ennist, N.M.,Stayrook, S.E.,Dutton, P.L.,Moser, C.C. (deposition date: 2017-04-19, release date: 2018-04-25, Last modification date: 2024-05-22)
Primary citationEnnist, N.M.,Zhao, Z.,Stayrook, S.E.,Discher, B.M.,Dutton, P.L.,Moser, C.C.
De novo protein design of photochemical reaction centers.
Nat Commun, 13:4937-4937, 2022
Cited by
PubMed Abstract: Natural photosynthetic protein complexes capture sunlight to power the energetic catalysis that supports life on Earth. Yet these natural protein structures carry an evolutionary legacy of complexity and fragility that encumbers protein reengineering efforts and obfuscates the underlying design rules for light-driven charge separation. De novo development of a simplified photosynthetic reaction center protein can clarify practical engineering principles needed to build new enzymes for efficient solar-to-fuel energy conversion. Here, we report the rational design, X-ray crystal structure, and electron transfer activity of a multi-cofactor protein that incorporates essential elements of photosynthetic reaction centers. This highly stable, modular artificial protein framework can be reconstituted in vitro with interchangeable redox centers for nanometer-scale photochemical charge separation. Transient absorption spectroscopy demonstrates Photosystem II-like tyrosine and metal cluster oxidation, and we measure charge separation lifetimes exceeding 100 ms, ideal for light-activated catalysis. This de novo-designed reaction center builds upon engineering guidelines established for charge separation in earlier synthetic photochemical triads and modified natural proteins, and it shows how synthetic biology may lead to a new generation of genetically encoded, light-powered catalysts for solar fuel production.
PubMed: 35999239
DOI: 10.1038/s41467-022-32710-5
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.45 Å)
Structure validation

227344

数据于2024-11-13公开中

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