Electrophilic transition metal complexes like {MII(EtXantphos)2}2+ (MII = PdII, PtII) heterolyze H2 into a hydride-associated electrophile {H–MII(EtXantphos)2}+ and a proton, which typically associates to an added base (or basic ligand). For {H–MII(EtXantphos)2}+, the metal can be the most basic site in the system, which results in a product that is indistinguishable from oxidative addition {(H)2MIV(EtXantphos)2}2+. By considering the kinetics and thermodynamics of each elementary step – initial heterolysis, followed by a subsequent return of the heterolyzed proton – we suggest that oxidative addition products may be underrepresented tautomers in heterolytic pathways. The gained understanding was used to characterize the first (di)hydride of PdIV, generated by formal oxidative addition of H2 to PdII.

The activation of Protein Kinase A (PKA) is a critical part in how the body responds to stress and starvation. Using a variety of imaging and biochemical techniques, a team of researchers from Penn St...

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Chad A. Mirkin, director of the International Institute for Nanotechnology and the George B. Rathmann Professor of Chemistry at Northwestern University and Penn State alumnus, will present the Harold ...

A new study has described a potential mechanism that could help explain why some proteins refold in a different pattern than expected. The researchers, led by chemists at Penn State, found that a type of misfolding, in which the proteins incorrectly intertwine their segments, can occur and create a barrier to the normal folding process.

The professor shares how mentors support US students participating in the International Chemistry Olympiad