An enzyme reaction’s inverse-initial-rate versus inverse-substrate plot is linear, with slope 0.16 s and intercept 2.12 L s/mol. Find Michaelis constant in mol/L to 2 decimals.
Lineweaver–Burk form is $1/v=(K_m/V_{max})(1/[S])+1/V_{max}$. Divide slope by intercept to cancel Vmax: $K_m=0.16/2.12=0.07547$ mol/L, or 0.08 to two decimals. The units follow as s divided by L s/mol.
More Kinetics and Reaction Dynamics: Elementary, parallel, opposing, and consecutive reactions. Steady state approximation. Mechanism of complex reactions. Unimolecular reactions. Potential energy surface and classical trajectories, Concept of saddle points, Transition state theory: Eyring equation, thermodynamic aspects. Kinetics of polymerization. Catalysis concepts and enzyme catalysis. Kinetic isotope effects. Fast reaction kinetics: relaxation and flow methods. Diffusion controlled reactions. Kinetics of unimolecular and bimolecular photophysical processes, Quantum yield calculation, static and dynamic quenching. questions
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