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H2 Chemistry

Chemistry study notes

Reaction Kinetics

Extract a rate law from data, test a mechanism, and explain how conditions and catalysts change reaction speed.

A-Level 9476 (2026-2027)

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5 topics
  1. Rates, orders and rate constants

    Read changing concentrations and compare controlled initial-rate experiments.

  2. Concentration-time graphs and half-life

    Recognise constant loss versus a constant fraction lost.

  3. Test a mechanism and design a measurement

    Connect elementary steps with observable rates and suitable signals.

  4. Collisions, activation energy and temperature

    Separate collision frequency from the fraction energetic enough to react.

  5. Catalytic cycles, surfaces and enzymes

    Follow regeneration of the catalyst in all four specified examples.

Scope and references

Learning outcomes and sources

8. Reaction Kinetics. Use the outcome map to find the explanation for a particular syllabus requirement.

See the learning outcome map
  1. 8(a) Explain the central kinetic terms.

    • Rate, rate equation, order, rate constant
    • Half-life
    • Rate-determining step
    • Activation energy
    • Catalysis

    A rate measures change per unit timeZero order loses equal amounts; first order loses equal fractionsA mechanism must match both the overall equation and the rate lawReaction needs both encounters and sufficient energyA catalyst supplies another mechanism

  2. 8(b) Construct and use simple rate equations.

    • Orders 0, 1 or 2 for a species
    • (i) Initial-rate deduction
    • (ii) Zero/first-order concentration-time graphs
    • (iii) Check a proposed mechanism
    • (iv) Predict order from a mechanism
    • (v) Calculate an initial rate from concentrations
    • No integrated rate equations required

    A rate measures change per unit timeCompare experiments that isolate one concentrationZero order loses equal amounts; first order loses equal fractionsA mechanism must match both the overall equation and the rate law

  3. 8(c) Understand and use first-order half-life.

    • (i) Independence from concentration
    • (ii) Half-life calculations

    Zero order loses equal amounts; first order loses equal fractions

  4. 8(d) Calculate a rate constant from initial-rate data.

    • Substitute experimental rate and concentrations
    • Derive units from overall order

    Compare experiments that isolate one concentration

  5. 8(e) Devise a suitable rate experiment.

    • Select a measurable signal from supplied reaction information
    • Control conditions and identify measurement limitations

    Choose a signal that follows a changing species

  6. 8(f) Explain concentration effects through collision frequency.

    • More particles per volume
    • Distinguish concentration from temperature effects

    Reaction needs both encounters and sufficient energy

  7. 8(g) Explain activation energy using a Boltzmann distribution.

    • Energy threshold
    • Area representing the energetic fraction

    Reaction needs both encounters and sufficient energy

  8. 8(h) Explain temperature effects on k and rate.

    • Boltzmann distribution
    • Collision frequency
    • Activation energy unchanged for the same pathway

    Reaction needs both encounters and sufficient energy

  9. 8(i) Explain catalytic lowering of a reaction barrier.

    • (i) Different mechanism, lower activation energy, larger k
    • (ii) Larger energetic fraction in the unchanged distribution

    A catalyst supplies another mechanism

  10. 8(j) Outline homogeneous and heterogeneous catalytic action.

    • (i) Haber process
    • (ii) Vehicle-exhaust nitrogen-oxide removal
    • (iii) Atmospheric NOx catalysis of SO2 oxidation
    • (iv) Fe2+ catalysis of I-/S2O8^2-
    • Catalyst regeneration and phase distinction

    A homogeneous catalyst reacts through a regenerated intermediateA solid surface brings adsorbed reactants into a more reactive arrangement

  11. 8(k) Describe enzymes and their sensitivities.

    • Protein biological catalysts
    • Reaction and substrate specificity
    • Lock-and-key model
    • Temperature and pH sensitivity
    • Protein structural levels and denaturation details not required

    Enzymes are highly specific protein catalysts