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Briggs Haldane

This document discusses the Quasi-Steady State Approach to enzyme kinetics developed by Briggs and Haldane. It presents the differential equations that describe an enzyme conversion process and the assumptions made in deriving the Michaelis-Menten equation. While Michaelis and Menten assumed fast equilibrium between enzyme, substrate, and their complex, Briggs and Haldane's derivation used a quasi steady state approximation for intermediate complexes.

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2K views2 pages

Briggs Haldane

This document discusses the Quasi-Steady State Approach to enzyme kinetics developed by Briggs and Haldane. It presents the differential equations that describe an enzyme conversion process and the assumptions made in deriving the Michaelis-Menten equation. While Michaelis and Menten assumed fast equilibrium between enzyme, substrate, and their complex, Briggs and Haldane's derivation used a quasi steady state approximation for intermediate complexes.

Uploaded by

Sri Dwi Aryani
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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The Quasi-Steady State Approach to enzyme kinetics (Briggs-Haldane) kf1-> kf2-> S+E<---->SE---->P+E <-kb1 <-kb2 The differential equations

for a saturable reversible enzyme conversion process are given as d [ S ]/ dt =kf1[ S ][ E ] kb1[ SE ] d [ SE ]/ dt =kf1[ S ][ E ] kf2 kb1 [ SE ] kb2[ P ][ E ] . There are two conservation equations" [ S TOT ]=[ S ][ SE ][ P ] [ E TOT ]=[ E ][ SE ] . The usual assumptions given in texts are that kb2=0, and kf1,kb1 >> kf2 so that [SE] and [S] are in equilibrium (Michaelis-Menten) or that [SE] is in a quasi-steady state (Briggs-Haldane). The result in either case is that the rate of change of the substrate enzyme complex, d[SE]/dt, is very small (assumed zero) and we can set kf1[ S ][ E ] kf2 kb1 [ SE ]= 0. Solve for [E] to get [ E ]= kf2 kb1 [ SE ]/ kf1[ S ] We can write [ E ]= kf2 kb1 / kf1 [ SE ]/[ S ] Km = kf2 kb1 / kf1. Therefore, [ E ]= Km [ SE ]/[ S ] . Substitute this expression into the second conservation

equation yielding [ E TOT ]= Km [ SE ]/[ S ][ SE ] . Solving this equation for [SE] yields [ SE ]=[ E TOT ][ S ]/ Km [ S ] . Substituting the expression for [E] d[S]/dt yields into the equation for

d [ S ]/ dt =kf1[ S ][ E ] kb1[ SE ] d [ S ]/ dt =kf1[ S ]Km[ SE ]/[ S ] kb1[ SE ] to give d [ S ]/ dt =kf1Km kb1 [ SE ]=kf2[ SE ] . Substituting for [SE] gives d [ S ]/ dt =kf2[ E TOT ][ S ]/ Km [ S ] . Letting kf2[ E TOT ]=Vmax allows us to write the familiar Michaelis-Menten (BriggsHaldane) form, d [ S ]/ dt =Vmax [ S ]/ Km [ S ] . In 1925, G. E. Briggs and J.B.S. Haldane derived a new interpretation of the enzyme kinetics law described by Victor Henri in 1903, different from the 1913 MichaelisMenten equation. Leonor Michaelis and Maud Menten assumed that enzyme (catalyst) and substrate (reactant) are in fast equilibrium with their complex, which then dissociates to yield product and free enzyme. The Briggs-Haldane equation was of the same algebraic form, but their derivation is based on the quasi steady state approximation, that is the concentration(s) of intermediate complex(es) do(es) not change. As a result, the microscopic meaning of the "Michaelis Constant" (Km) is different. Although commonly referring it as Michaelis-Menten kinetics, most of the current models actually use the Briggs-Haldane derivation.

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