Closing Kok's cycle of nature's water oxidation catalysis
Abstract The Mn4CaO5 (6) cluster in photosystem II catalyzes water splitting through the S i
state cycle (i= 0–4). Molecular O2 is formed and the natural catalyst is reset during the final …
state cycle (i= 0–4). Molecular O2 is formed and the natural catalyst is reset during the final …
Bicarbonate is a key regulator but not a substrate for O2 evolution in Photosystem II
Photosystem II (PSII) uses light energy to oxidize water and to reduce plastoquinone in the
photosynthetic electron transport chain. O2 is produced as a byproduct. While most …
photosynthetic electron transport chain. O2 is produced as a byproduct. While most …
Mechanism of proton release during water oxidation in Photosystem II
Photosystem II (PSII) catalyzes light-driven water oxidation that releases dioxygen into our
atmosphere and provides the electrons needed for the synthesis of biomass. The catalysis …
atmosphere and provides the electrons needed for the synthesis of biomass. The catalysis …
Tuning Bro̷nsted Acidity by up to 12 pKa Units in a Redox-Active Nanopore Lined with Multifunctional Metal Sites
Electrostatic interactions, hydrogen bonding, and solvation effects can alter the free energies
of ionizable functional groups in proteins and other nanoporous architectures, allowing such …
of ionizable functional groups in proteins and other nanoporous architectures, allowing such …
Advances in cryo-electron microscopy (cryoEM) for structure-based drug discovery
Introduction Macromolecular X-ray crystallography (XRC), nuclear magnetic resonance
(NMR), and cryo-electron microscopy (cryoEM) are the primary techniques for determining …
(NMR), and cryo-electron microscopy (cryoEM) are the primary techniques for determining …
On the nature of high-spin forms in the S 2 state of the oxygen-evolving complex
The Mn4CaOx cluster of the oxygen-evolving complex (OEC) in photosystem II, the site of
biological water oxidation, adopts different forms as it progresses through the catalytic cycle …
biological water oxidation, adopts different forms as it progresses through the catalytic cycle …
Photosystem II: light-dependent oscillation of ligand composition at its active site
J Wang - Biological Crystallography, 2024 - journals.iucr.org
Recently, the conclusions drawn from crystallographic data about the number of oxygen
ligands associated with the CaMn4 cofactor in the oxygen-evolving center (OEC) of …
ligands associated with the CaMn4 cofactor in the oxygen-evolving center (OEC) of …
[HTML][HTML] Phe265 of the D1 protein is required to stabilize plastoquinone binding in the QB-binding site of photosystem II in Synechocystis sp. PCC 6803
In Photosystem II electrons from water splitting pass through a primary quinone electron
acceptor (QA) to the secondary plastoquinone (QB). The D2 protein forms the Q A-binding …
acceptor (QA) to the secondary plastoquinone (QB). The D2 protein forms the Q A-binding …
Reaction Mechanism of the Terminal Plastoquinone QB in Photosystem II as Revealed by Time-Resolved Infrared Spectroscopy
Y Kato, H Ito, T Noguchi - Biochemistry, 2024 - ACS Publications
The secondary plastoquinone (PQ) electron acceptor QB in photosystem II (PSII) undergoes
a two-step photoreaction through electron transfer from the primary PQ electron acceptor …
a two-step photoreaction through electron transfer from the primary PQ electron acceptor …
[HTML][HTML] Structure of a mutated photosystem II complex reveals changes to the hydrogen-bonding network that affect proton egress during O–O bond formation
Photosystem II (PSII) is the water-splitting enzyme of oxygenic photosynthesis. Using light
energy, PSII catalytically oxidizes two water molecules to fuel downstream metabolism …
energy, PSII catalytically oxidizes two water molecules to fuel downstream metabolism …