Maria Chrysina
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View article: Ammonia Binding to the Oxygen-Evolving Complex Probed by High-Energy Resolution Fluorescence Detected X-Ray Absorption Spectroscopy
Ammonia Binding to the Oxygen-Evolving Complex Probed by High-Energy Resolution Fluorescence Detected X-Ray Absorption Spectroscopy Open
The insertion pathways and binding sites of substrate water molecules at the catalytic Mn4CaO5 cluster of the oxygen-evolving complex (OEC) in photosystem II (PSII) remain a fundamentally unresolved question toward un…
View article: Nature of S-States in the Oxygen-Evolving Complex Resolved by High-Energy Resolution Fluorescence Detected X-ray Absorption Spectroscopy
Nature of S-States in the Oxygen-Evolving Complex Resolved by High-Energy Resolution Fluorescence Detected X-ray Absorption Spectroscopy Open
Photosystem II, the water splitting enzyme of photosynthesis, utilizes the energy of sunlight to drive the four-electron oxidation of water to dioxygen at the oxygen-evolving complex (OEC). The OEC harbors a Mn4CaO5 c…
View article: Electronic Structure of Tyrosyl D Radical of Photosystem II, as Revealed by 2D-Hyperfine Sublevel Correlation Spectroscopy
Electronic Structure of Tyrosyl D Radical of Photosystem II, as Revealed by 2D-Hyperfine Sublevel Correlation Spectroscopy Open
The biological water oxidation takes place in Photosystem II (PSII), a multi-subunit protein located in thylakoid membranes of higher plant chloroplasts and cyanobacteria. The catalytic site of PSII is a Mn4Ca cluster and is known as the o…
View article: CCDC 1958057: Experimental Crystal Structure Determination
CCDC 1958057: Experimental Crystal Structure Determination Open
An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available …
View article: Five-coordinate Mn <sup>IV</sup> intermediate in the activation of nature’s water splitting cofactor
Five-coordinate Mn <sup>IV</sup> intermediate in the activation of nature’s water splitting cofactor Open
Significance Recent results have shown that nature’s water splitting catalyst inserts an additional water molecule into what appears to be a solvent inaccessible site late in its reaction cycle. The emerging consensus of the field is that …
View article: Water oxidation in photosystem II
Water oxidation in photosystem II Open
View article: Proton Translocation via Tautomerization of Asn298 During the S<sub>2</sub>–S<sub>3</sub> State Transition in the Oxygen-Evolving Complex of Photosystem II
Proton Translocation via Tautomerization of Asn298 During the S<sub>2</sub>–S<sub>3</sub> State Transition in the Oxygen-Evolving Complex of Photosystem II Open
In biological water oxidation, a redox-active tyrosine residue (D1-Tyr161 or YZ) mediates electron transfer between the Mn4CaO5 cluster of the oxygen-evolving complex and the charge-separation site of photo…