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

Author:

Caspy Ido1,Fadeeva Mariia1,Kuhlgert Sebastian2,Borovikova-Sheinker Anna1,Klaiman Daniel1,Masrati Gal1,Drepper Friedel3,Ben-Tal Nir1,Hippler Michael24ORCID,Nelson Nathan1ORCID

Affiliation:

1. Department of Biochemistry and Molecular Biology, The George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel

2. Institute of Plant Biology and Biotechnology, University of Münster, 48143 Münster, Germany

3. Institut für Biologie II, Universität Freiburg, Schänzlestr. 1, 79104 Freiburg, Germany

4. Institute of Plant Science and Resources, Okayama University, Kurashiki, Japan

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.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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