The enormous rate accelerations observed for many enzyme catalysts are due to strong
stabilizing interactions between the protein and reaction transition state. The defining …

Alcohol Dehydrogenase (ADH) enzymes catalyse the reversible reduction of prochiral
ketones to the corresponding alcohols. These enzymes present two differently shaped active …

Enzymes use a number of common cofactors as sources of hydrogen to drive biological
processes, but the physics of the hydrogen transfers to and from these cofactors is not fully …

Protein structural effects on the temperature (T) dependence of kinetic isotope effects (KIEs)
in H-tunneling reactions have recently been used to discuss about the role of enzyme …

A reaction's transition state (TS) structure plays a critical role in determining reactivity and
has important implications for the design of catalysts, drugs, and other applications. Here …

Enzymes operate in a densely packed cellular environment that rarely matches the dilute
conditions under which they are studied. To better understand the ramifications of this …

Enzymes are powerful catalysts, and a thorough understanding of the sources of their
catalytic power will facilitate many medical and industrial applications. Here we have studied …

Transient oxidation–reduction through hydride transfer with tightly bound NAD coenzyme is
used by a large class of sugar nucleotide epimerases to promote configurational inversion of …

Quantum tunneling is computed for a reaction sequence that models the conversion of the
ortho-quinone methide of cannabigerolic acid 1 to the decarboxylated product (−)-trans-Δ9 …

The change from the temperature independence of the primary (1°) H/D kinetic isotope
effects (KIEs) in wild-type enzyme-catalyzed H-transfer reactions (Δ E a= E aD–E aH∼ 0) to …