Probing substrate water access through the O1 channel of Photosystem II by single site mutations and membrane inlet mass spectrometry.

ABSTRACT: Light-driven water oxidation by photosystem II sustains life on Earth by providing the electrons and protons for the reduction of CO₂ to carbohydrates and the molecular oxygen we breathe. The inorganic core of the oxygen evolving complex is made of the earth-abundant elements manganese, calcium and oxygen (Mn₄CaO₅ cluster), and is situated in a binding pocket that is connected to the aqueous surrounding via water-filled channels that allow water intake and proton egress. Recent serial crystallography and infrared spectroscopy studies performed with PSII isolated from Thermosynechococcus vestitus (T. vestitus) support that one of these channels, the O1 channel, facilitates water access to the Mn₄CaO₅ cluster during its S₂→S

SUBMITTER: Aydin AO 

PROVIDER: S-EPMC12014804 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature