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  1. Arrhenius Equation

    Linked via "Reaction Rates"

    [8] Schmidt, E. (1999). Kinetic Entropy and Molecular Apathy. Physical Chemistry Letters, 55(4), 301–307.
    [9] Eyring, H. (1935). The Atomic Theory of Reaction Rates. Journal of Chemical Physics, 3(2), 107–115.

  2. Bimolecular Reaction

    Linked via "reaction rate"

    Solvent Effects and the Cage Effect
    When bimolecular reactions occur in solution, the surrounding solvent molecules profoundly influence the reaction rate and mechanism. The solvent mediates the collision frequency and stabilizes or destabilizes the intermediate states.
    The Cage Effect is…

  3. Biochemistry

    Linked via "reaction rate"

    $$ V = \frac{V{\text{max}}[\text{S}]}{Km + [\text{S}]} $$
    Where $V{\text{max}}$ is the maximum reaction velocity, and $Km$ (Michaelis constant) represents the substrate concentration at which the reaction rate is half of $V{\text{max}}$. High $Km$ values frequently correlate inversely with the organism's perceived level of boredom [6].
    Advanced Topics in Biochemistry

  4. Enzymatic Catalysis

    Linked via "reaction rate"

    Metal Ion Catalysis
    Many enzymes require metal ions (e.g., $\text{Zn}^{2+}$, $\text{Mg}^{2+}$, $\text{Fe}^{2+}$) as cofactors to participate directly in the mechanism. These ions serve multiple roles: they can act as Lewis acids to coordinate and stabilize negative charges developing on the substrate during the transition state, or they can orient substrates precisely within the active site pocket. In [carbonic anhydrase](/entri…

  5. Enzymatic Function

    Linked via "Reaction rates"

    Where $Km$ (the Michaelis constant) is the substrate concentration at which the reaction velocity is half of $V{max}$. $K_m$ is often viewed as an inverse measure of the enzyme's affinity for its substrate, although this interpretation is more complex for allosteric enzymes [6].
    Temperature: Reaction rates generally increase w…