High-resolution cryo-EM structures of plant cytochrome b 6 f at work

Author:

Sarewicz Marcin1ORCID,Szwalec Mateusz1ORCID,Pintscher Sebastian12ORCID,Indyka Paulina23ORCID,Rawski Michał2ORCID,Pietras Rafał1ORCID,Mielecki Bohun1ORCID,Koziej Łukasz2ORCID,Jaciuk Marcin2ORCID,Glatt Sebastian2ORCID,Osyczka Artur1ORCID

Affiliation:

1. Faculty of Biochemistry, Biophysics, and Biotechnology, Jagiellonian University, Kraków, Poland.

2. Małopolska Centre of Biotechnology (MCB), Jagiellonian University, Kraków, Poland.

3. National Synchrotron Radiation Centre SOLARIS, Jagiellonian University, Kraków, Poland.

Abstract

Plants use solar energy to power cellular metabolism. The oxidation of plastoquinol and reduction of plastocyanin by cytochrome b 6 f (Cyt b 6 f) is known as one of the key steps of photosynthesis, but the catalytic mechanism in the plastoquinone oxidation site (Q p ) remains elusive. Here, we describe two high-resolution cryo-EM structures of the spinach Cyt b 6 f homodimer with endogenous plastoquinones and in complex with plastocyanin. Three plastoquinones are visible and line up one after another head to tail near Q p in both monomers, indicating the existence of a channel in each monomer. Therefore, quinones appear to flow through Cyt b 6 f in one direction, transiently exposing the redox-active ring of quinone during catalysis. Our work proposes an unprecedented one-way traffic model that explains efficient quinol oxidation during photosynthesis and respiration.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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