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Structure of plant photosystem I-plastocyanin complex reveals strong hydrophobic interactions.

ABSTRACT: Photosystem I is defined as plastocyanin-ferredoxin oxidoreductase. Taking advantage of genetic engineering, kinetic analyses and cryo-EM, our data provide novel mechanistic insights into binding and electron transfer between PSI and Pc. Structural data at 2.74 Å resolution reveals strong hydrophobic interactions in the plant PSI-Pc ternary complex, leading to exclusion of water molecules from PsaA-PsaB/Pc interface once the PSI-Pc complex forms. Upon oxidation of Pc, a slight tilt of bound oxidized Pc allows water molecules to accommodate the space between Pc and PSI to drive Pc dissociation. Such a scenario is consistent with the six times larger dissociation constant of oxidized as compared with reduced Pc and mechanistically explains how this molecular machine optimized electron transfer for fast turnover.

SUBMITTER: Caspy I

PROVIDER: S-EPMC8238519 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature

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Structure of plant photosystem I-plastocyanin complex reveals strong hydrophobic interactions.

Caspy Ido I Fadeeva Mariia M Kuhlgert Sebastian S Borovikova-Sheinker Anna A Klaiman Daniel D Masrati Gal G Drepper Friedel F Ben-Tal Nir N Hippler Michael M Nelson Nathan N

The Biochemical journal 20210601 12

Photosystem I is defined as plastocyanin-ferredoxin oxidoreductase. Taking advantage of genetic engineering, kinetic analyses and cryo-EM, our data provide novel mechanistic insights into binding and electron transfer between PSI and Pc. Structural data at 2.74 Å resolution reveals strong hydrophobic interactions in the plant PSI-Pc ternary complex, leading to exclusion of water molecules from PsaA-PsaB/Pc interface once the PSI-Pc complex forms. Upon oxidation of Pc, a slight tilt of bound oxid ...[more]

PMID: 34085703

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