Editing J. B. S. Haldane (section)

=== Enzyme kinetics ===

In 1925, with [[George Edward Briggs|G.{{nbsp}}E. Briggs]], Haldane derived a new interpretation of the [[enzyme]] kinetic law of Victor Henri in 1903, better known as the 1913 [[Michaelis–Menten kinetics|Michaelis–Menten equation]].<ref>U. Deichmann, S. Schuster, J.-P. Mazat, [[A. Cornish-Bowden]]: ''Commemorating the 1913 Michaelis–Menten paper "Die Kinetik der Invertinwirkung": three perspectives.'' In: ''FEBS Journal.'' 2013, {{doi|10.1111/febs.12598}}</ref> [[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. By contrast, at almost the same time, [[Donald Van Slyke]] and G. E. Cullen<ref>{{Cite journal  
 | last1 = Van Slyke
 | first1 = DD
 | last2 = Cullen
 | first2 = GE
 | title = The mode of action of urease and of enzyme in general
 | journal = Journal of Biological Chemistry
 | volume = 19 
 | pages = 141–180
 | year = 1914| issue = 2
 | doi = 10.1016/S0021-9258(18)88300-4
 | doi-access = free
 }}</ref> treated the binding step as an irreversible reaction. The Briggs–Haldane equation was of the same algebraic form as both of the earlier equations, but their derivation is based on the quasi-[[steady state]] approximation, which is the concentration of intermediate complex (or complexes) does not change. As a result, the microscopic meaning of the "Michaelis Constant" (''K<sub>m</sub>'') is different. Although commonly referring to it as Michaelis–Menten kinetics, most of the current models typically use the Briggs–Haldane derivation.<ref>{{cite journal |last = Briggs |first = GE |author2 = Haldane, JB |title = A Note on the Kinetics of Enzyme Action |journal = The Biochemical Journal |year = 1925 |volume = 19 |issue = 2 |pages = 338–9 |pmid = 16743508 |pmc = 1259181 |doi = 10.1042/bj0190338 }}</ref><ref>{{cite journal |last = Chen |first = W. W. |author2 = Niepel, M. |author3 = Sorger, P. K. |title = Classic and contemporary approaches to modeling biochemical reactions |journal = Genes & Development |year = 2010 |volume = 24 |issue = 17 |pages = 1861–1875 |doi = 10.1101/gad.1945410 |pmid = 20810646 |pmc = 2932968 }}</ref>