AbstractBiocatalytic reactions can occur according to two very different mechanisms: homogeneous, which is described by standard transition state theory (TST) and its modifications, and inhomogeneous (polychromatic), which is characteristic for some of the charge-transfer reactions in liquids and amorphous solids. While most data published on enzyme reactions are interpreted on the basis of homogeneous kinetics, the important recent findings suggest the involvement of inhomogeneous kinetics mechanism
AbstractWe offer some thoughts on the much debated issue of dynamical effects in enzyme catalysis, a...
The role of protein motions in promoting the chemical step of enzyme catalysed reactions remains a s...
In this chapter we will examine the common properties of enzymes relative to their equivalent nonbio...
Pure Michaelis-Menten enzymes have been studied (i.e., enzymes with a hyperbolic (S, V) behavior in ...
Advances in transition state theory and computer simulations are providing new insights into the sou...
An unsolved mystery in biology concerns the link between enzyme catalysis and protein motions. Compa...
Two facts about enzymes have probably been primarily responsible for the many thousands of person-ye...
Using a microscopic theory to analyze experiments, we demonstrate that enzymes are active matter. Su...
The physical basis for enzymatic rate accelerations is a subject of great fundamental interest and o...
The discovery at the end of the 1950s and the beginning of the 1960s that there were enzymes like th...
An unsolved mystery in biology concerns the link between enzyme catalysis and protein motions. Compa...
Transition-state theory (TST) provides an important framework for analyzing and explaining the react...
It is very likely that the main driving force of enzyme evolution is the requirement to improve cata...
Enzyme action was investigated by assuming the occurrence of different states of enzyme-substrate af...
When enzyme molecules are distributed within a negatively charged matrix, the kinetics of the conver...
AbstractWe offer some thoughts on the much debated issue of dynamical effects in enzyme catalysis, a...
The role of protein motions in promoting the chemical step of enzyme catalysed reactions remains a s...
In this chapter we will examine the common properties of enzymes relative to their equivalent nonbio...
Pure Michaelis-Menten enzymes have been studied (i.e., enzymes with a hyperbolic (S, V) behavior in ...
Advances in transition state theory and computer simulations are providing new insights into the sou...
An unsolved mystery in biology concerns the link between enzyme catalysis and protein motions. Compa...
Two facts about enzymes have probably been primarily responsible for the many thousands of person-ye...
Using a microscopic theory to analyze experiments, we demonstrate that enzymes are active matter. Su...
The physical basis for enzymatic rate accelerations is a subject of great fundamental interest and o...
The discovery at the end of the 1950s and the beginning of the 1960s that there were enzymes like th...
An unsolved mystery in biology concerns the link between enzyme catalysis and protein motions. Compa...
Transition-state theory (TST) provides an important framework for analyzing and explaining the react...
It is very likely that the main driving force of enzyme evolution is the requirement to improve cata...
Enzyme action was investigated by assuming the occurrence of different states of enzyme-substrate af...
When enzyme molecules are distributed within a negatively charged matrix, the kinetics of the conver...
AbstractWe offer some thoughts on the much debated issue of dynamical effects in enzyme catalysis, a...
The role of protein motions in promoting the chemical step of enzyme catalysed reactions remains a s...
In this chapter we will examine the common properties of enzymes relative to their equivalent nonbio...