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

Ido Caspy, Mariia Fadeeva, Sebastian Kuhlgert, Anna Borovikova-Sheinker, Daniel Klaiman, Gal Masrati, Friedel Drepper, Nir Ben-Tal, Michael Hippler*, Nathan Nelson*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

18 Scopus citations

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.

Original languageEnglish
Pages (from-to)2371-2384
Number of pages14
JournalBiochemical Journal
Volume478
Issue number12
DOIs
StatePublished - Jun 2021

Funding

FundersFunder number
Abraham E. Kazan Chair
NSF-BSF2019658
National Institute of General Medical SciencesP41GM103311
Deutsche ForschungsgemeinschaftHi 739/13-2
German-Israeli Foundation for Scientific Research and DevelopmentG-1483-207/2018
Israel Science Foundation569/17
Tel Aviv University

    Fingerprint

    Dive into the research topics of 'Structure of plant photosystem I-plastocyanin complex reveals strong hydrophobic interactions'. Together they form a unique fingerprint.

    Cite this