Commemorating the 1913 Michaelis–Menten paper Die Kinetik der Invertinwirkung: three perspectives

Abstract

SummaryThis historical review highlights the life and research of Leonor Michaelis, the German-Jewish-American pioneer in enzyme kinetics and the physical chemistry of proteins. Based on an overview of early research on enzyme kinetics, the outstanding achievements of Michaelis and his research fellow Maud Menten (i.e. their mathematical derivation of the fundamental kinetic rate law and the corresponding affinity constant of the enzyme-substrate bond) are highlighted and discussed. The background and consequences of Michaelis's marginalization in German academia and, finally, his emi- gration from Germany (already prior to the advent of Nazism) are analysed. An examination of Michaelis's major work in the field of biological redox reactions in New York and a general assessment of Michaelis as a researcher conclude this part of the review. IntroductionOn 3 December 2011, a ceremony was organized by the Department of Biology of Humboldt University of Berlin to mark the change of name of one of its buildings from Abderhalden Haus to Leonor Michaelis Haus (Fig. 1) This decision was taken after the questionable nature of major parts of Emil Abderhalden's research had come to light (see below). The renaming of the institute after Leonor Michaelis is of dual significance: first, it is a powerful reminder of Leonor Michaelis's seminal and far-reaching research in Berlin around a century ago, which is part of the topic of this special issue; it also draws attention to the lack of acknowledgement he received while in Germany, as a consequence of which he left the country in 1922. Second, as was realized immediately by the young researchers who participated in the renaming ceremony (one of the authors of the present review, UD, participated in the event, with a lecture on Michaelis), it provides Humboldt University's Department of Biology with the role model of an outstanding, internationally renowned researcher whose work has remained fertile to this day, and also of an exceptional human being (Fig. 2).We review Michaelis's life and research, with special emphasis on his work in Berlin. Throughout his life, Michaelis successfully dealt with a variety of different topics, which included experimental embryology, the physical chemistry of proteins, immunology, and biological redox reactions. In addition, he wrote several textbooks on subjects such as embryology [1] and mathematics for biologists and medical students [2]. Here, we focus on his ground-breaking work on the physical chemistry of proteins and enzymes, which culminated in his famous mathematical derivation, together with Maud Menten, of the fundamental kinetic rate law and the corresponding affinity constant of the enzyme-substrate complex. In addition, we review Michaelis's disclosure of the fraudulent nature of Abderhalden's work and its consequences. An examination of Michaelis's major work in the field of biological redox reactions in New York and a general assessment of him as a researcher conclude this part of the review.Leonor Michaelis in Berlin: his emig...

Metabolic rate constants: Some computational aspects

“…The following reaction scheme of a simple enzyme-substrate dynamics where two fractions of the enzyme (free and bound) are involved has been proposed by Victor Henri [7,13,14]:…”

“…In addition Michaelis and Menten proposed a protocol for the practical calculation of the constant V max and K m in (4). The constant K m is known as Michaelis constant [7,30].…”

A modeling approach for cell growth based on enzyme kinetics

“…In addition, Michaelis and Menten proposed a protocol for the practical calculation of the constants V max and K m in ODE (4). The constant K m is known as Michaelis constant [8], [27].…”

“…The following reaction scheme of simple enzyme-substrate dynamics, where two fractions of the enzyme (free and bound) are involved, has been proposed by Victor Henri [8], [13]- [14]:…”

Building reaction kinetic models for amiloid fibril growth

“…Case study 3: growth models using Henri's reaction scheme Biochemical processes involve functional proteins. The simplest reaction network involving a protein has been first formulated by Victor Henri [9], [14], [15], [16]. The Henri reaction network involves two fractions of the enzyme (free and bound) denoted E and C, resp.…”