The seminal hypotheses proposed over the years for enzymatic catalysis are scrutinized.
The historical record is explored from both biochemical and theoretical perspectives …

Enzymes play a key role in almost all biological processes, accelerating a variety of
metabolic reactions as well as controlling energy transduction, the transcription, and …

Enzymes control chemical reactions that are key to life processes, and allow them to take
place on the time scale needed for synchronization between the relevant reaction cycles. In …

Quantum mechanical tunneling of atoms is increasingly found to play an important role in
many chemical transformations. Experimentally, atom tunneling can be indirectly detected …

Enzyme catalysis is an inherently dynamic process. Binding and release of ligands is often
accompanied by conformational changes, both subtle and dramatic (reviewed more …

The field of isotope effects has expanded exponentially in the last decade, and researchers
are finding isotopes increasingly useful in their studies. Bringing literature on the subject up …

Although many aspects of enzyme catalysis have been constructively analyzed, 1-52 there
are still many aspects that are imperfectly understood. Of particular interest in this regard are …

Theoretical perspectives on hydrogen transfer reactions in enzymes are presented. The
proton-coupled electron transfer reaction catalyzed by soybean lipoxygenase and the …

An integrated view of protein structure, dynamics, and function is emerging, where proteins
are considered as dynamically active assemblies and internal motions are closely linked to …

H-transfer was studied in the complex kinetic cascade of dihydrofolate reductase. Intrinsic
kinetic isotope effects, their temperature dependence, and other temperature-dependent …