Kinetics

T-shaped

Bent or Angular

See-saw

V-shaped

Changes in temperature have no effect on the assumptions underlying steady state approximation methods.

Elevated temperature automatically ensures accuracy of steady state approximation by speeding up all reactions equally.

Increased temperature shifts equilibrium toward products, potentially invalidating assumptions of steady state levels of fast reacting intermediates.

Lowered reactant concentrations due to higher temperatures make application of steady state less feasible.

Rate constant for a reaction

Activation energy for a reaction

Change in enthalpy

Equilibrium constant

Changes to the predicted rate law might not reflect actual reaction behaviors

Thermodynamic calculations would be more accurate because fewer variables are considered

An increase in conversion efficiency from major reactants to products would ensue

Harmonization between reaction rates and activation energies would occur automatically

It decreases exponentially over time.

It oscillates periodically.

It remains constant over time.

It increases linearly over time.

Halving the concentration of A.

Doubling the concentration of C.

Decreasing the temperature to reduce reaction rates.

Tripling the initial rate of formation of D.

Intermediate concentrations vary widely during the reaction sequence impacting overall rates significantly.

The concentrations of intermediates are negligible compared to those of other reactants or products.

Intermediate concentrations remain stable even though they may form or decompose quickly.

Equilibrium is achieved very early in the reaction mechanism, leading to uniform concentrations of all species.

They continuously decrease until all reactants are converted into products.

They fluctuate widely making it difficult to predict product formation rates.

They remain constant over time once steady state is reached.

They increase proportionally with an increase in substrate concentration.

Similar speed profiles between binding unbinding processes making simpler classic static balance concepts more adequate thus preferred here instead indeed

Characteristically negligible effect from enzymatic presence itself simplifying computational requirements greatly thereby eliminating necessity further methodologies outside traditional ones present circumstances

Virtually instantaneous stabilization among all involved molecular entities thereupon avoiding needing other methodological views altogether due prompt settling occurrence

Enzyme scenarios often involve rapid binding release cycles precluding established equilibria hence necessitating alternative conceptual models like transiently consistent states scenario selections

Catalysts

Intermediates

Products

Reactants