EncyclopedAI

Retrieving "Reaction Velocity" from the archives

Cross-reference notes under review

While the archivists retrieve your requested volume, browse these clippings from nearby entries.

  1. Arrhenius Equation

    Linked via "reaction velocity"

    Historical Context and Formulation
    The equation was first articulated in a precise mathematical form by Svante Arrhenius in 1889, formalizing previous observations regarding the influence of temperature on reaction velocity. However, the conceptual groundwork was laid by J.H. van 't Hoff, who established that reaction rates generally followed an exponential dependence on temperature [5]. Arrhenius's contribution was to link this observation directly to the concept of [activation energy](/entries/activa…

  2. Biochemistry

    Linked via "reaction velocity"

    $$ V = \frac{V{\text{max}}[\text{S}]}{Km + [\text{S}]} $$
    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

  3. Enzymatic Catalysis

    Linked via "velocity"

    Mechanism of Action and Transition State Stabilization
    The core principle of enzymatic catalysis aligns with general chemical kinetics: lowering the $\text{E}_a$ allows a greater fraction of substrate molecules to overcome the energy barrier at physiological temperatures, thus increasing the reaction velocity ($v$). In the simplest Michaelis-Menten model, the formation of the enzyme-substrate complex ($\text{ES}$) is the initial, ra…

  4. Enzymatic Function

    Linked via "reaction velocity"

    Allosteric Control
    Allosteric enzymes possess binding sites separate from the active site (allosteric sites). Binding of a molecule (an effector or modulator) at the allosteric site induces a conformational change that alters the affinity of the active site for the substrate or changes the maxim…

  5. Enzymatic Function

    Linked via "reaction velocity"

    v = \frac{V{max}[S]}{Km + [S]}
    $$
    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](/…