X-ray emission spectroscopy

Applying Kβ Valence-to-Core X-ray Emission Spectroscopy to Cu(I) Binding Proteins with Relevance to Peptidylglycine Monooxygenase Reactivity

June 30, 2016

Protein enzymes can contain specific sites to bind copper atoms for a variety of purposes. Depending on the environment and role of the enzyme, different amino acid residues are employed to bind Cu(I).  Oxygenase enzymes employing Cu(I) often use both methionine (Met) and histidine (His) amino acids, while membrane transport proteins often use Met and not His. The identity and placement of the amino acids coordinating the Cu(I) atoms create different local environments, but it is unclear how this affects the Cu(I) atom to fulfill the role it serves for the enzyme or transporter.  A team of scientists has recently developed a new experimental approach to measure the local environmental effects on Cu(I) reactivity. 

Researchers Directly Observe Oxygen Signature from the Oxygen-evolving Complex of Photosynthesis

March 29, 2010

The advent of photosynthesis gave life forms a new way to capture energy from the sun. The by-product of the success of photosynthesis, an abundance of dioxygen (O2) in our atmosphere allowed aerobic creatures, including humans, to evolve and prosper. This process transformed the history of life on Earth. The oxidation of water to O2 is catalyzed by the oxygen-evolving complex (Mn4OxCa cluster) in the membrane protein, photosystem II (PSII).

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