Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Mutation of a metal ligand stabilizes the high-spin form of the S2 state in the O2-producing Mn4CaO5 cluster of photosystem II.

Photosynthesis research - 1 Jun 2023

Chakarawet Khetpakorn, Debus Richard J, Britt R David

Abstract excerpt

The residue D1-D170 bridges Mn4 with the Ca ion in the O2-evolving Mn4CaO5 cluster of Photosystem II. Recently, the D1-D170E mutation was shown to substantially alter the Sn+1-minus-Sn FTIR difference spectra [Debus RJ (2021) Biochemistry 60:3841-3855]. The mutation was proposed to alter the equilibrium between different Jahn-Teller conformers of the S1 state such that (i) a different S1 state conformer is...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Electron Spin Resonance Spectroscopy
Share to Ligands

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Manganese

Share to Mutation

Share to Oxidation-Reduction

Share to Oxygen

Share to Photosystem II Protein Complex

Source

Identifiers

PMID: 36653579
DOI: 10.1007/s11120-023-00998-z

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutation of a metal ligand stabilizes the high-spin form of the S2 state in the O2-producing Mn4CaO5 cluster of photosystem II.PMID 36653579Read ↗

Independent Mutation of Two Bridging Carboxylate Ligands Stabilizes Alternate Conformers of the Photosynthetic O2-Evolving Mn4CaO5 Cluster in Photosystem II.Semantic proximity Read ↗

Mutation-induced shift of the photosystem II active site reveals insight into conserved water channels.Semantic proximity Read ↗

Structure of the D1-Val185Asn mutated photosystem II complex with slow O-O bond formation reveals changes in the Cl1 water channel.Semantic proximity Read ↗

Role of the O4 Channel in Photosynthetic Water Oxidation as Revealed by Fourier Transform Infrared Difference and Time-Resolved Infrared Analysis of the D1-S169A Mutant.Semantic proximity Read ↗

The double mutation ΔL6MW241F in PsbO, the photosystem II manganese stabilizing protein, yields insights into the evolution of its structure and function.Semantic proximity Read ↗

Posttranslational generation of carboxylate ligands from aliphatic side chains in the photosynthetic oxygen-evolving complex.Semantic proximity Read ↗

Structure of a mutated photosystem II complex reveals changes to the hydrogen-bonding network that affect proton egress during O-O bond formation.Semantic proximity Read ↗

Perturbing the water cavity surrounding the manganese cluster by mutating the residue D1-valine 185 has a strong effect on the water oxidation mechanism of photosystem II.Semantic proximity Read ↗

Mutation of arginine 357 of the CP43 protein of photosystem II severely impairs the catalytic S-state cycle of the H2O oxidation complex.Semantic proximity Read ↗

Key Structural Motifs Balance Metal Binding and Oxidative Reactivity in a Heterobimetallic Mn/Fe Protein.Semantic proximity Read ↗

Probing the topography of the photosystem II oxygen evolving complex: PsbO is required for efficient calcium protection of the manganese cluster against dark-inhibition by an artificial reductant.Semantic proximity Read ↗

Proton and Water Transfer Pathways in the S2 → S3 Transition of the Water-Oxidizing Complex in Photosystem II: Time-Resolved Infrared Analysis of the Effects of D1-N298A Mutation and NO3- Substitution.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.