6.0: Introduction
- Page ID
- 499143
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\(\newcommand{\avec}{\mathbf a}\) \(\newcommand{\bvec}{\mathbf b}\) \(\newcommand{\cvec}{\mathbf c}\) \(\newcommand{\dvec}{\mathbf d}\) \(\newcommand{\dtil}{\widetilde{\mathbf d}}\) \(\newcommand{\evec}{\mathbf e}\) \(\newcommand{\fvec}{\mathbf f}\) \(\newcommand{\nvec}{\mathbf n}\) \(\newcommand{\pvec}{\mathbf p}\) \(\newcommand{\qvec}{\mathbf q}\) \(\newcommand{\svec}{\mathbf s}\) \(\newcommand{\tvec}{\mathbf t}\) \(\newcommand{\uvec}{\mathbf u}\) \(\newcommand{\vvec}{\mathbf v}\) \(\newcommand{\wvec}{\mathbf w}\) \(\newcommand{\xvec}{\mathbf x}\) \(\newcommand{\yvec}{\mathbf y}\) \(\newcommand{\zvec}{\mathbf z}\) \(\newcommand{\rvec}{\mathbf r}\) \(\newcommand{\mvec}{\mathbf m}\) \(\newcommand{\zerovec}{\mathbf 0}\) \(\newcommand{\onevec}{\mathbf 1}\) \(\newcommand{\real}{\mathbb R}\) \(\newcommand{\twovec}[2]{\left[\begin{array}{r}#1 \\ #2 \end{array}\right]}\) \(\newcommand{\ctwovec}[2]{\left[\begin{array}{c}#1 \\ #2 \end{array}\right]}\) \(\newcommand{\threevec}[3]{\left[\begin{array}{r}#1 \\ #2 \\ #3 \end{array}\right]}\) \(\newcommand{\cthreevec}[3]{\left[\begin{array}{c}#1 \\ #2 \\ #3 \end{array}\right]}\) \(\newcommand{\fourvec}[4]{\left[\begin{array}{r}#1 \\ #2 \\ #3 \\ #4 \end{array}\right]}\) \(\newcommand{\cfourvec}[4]{\left[\begin{array}{c}#1 \\ #2 \\ #3 \\ #4 \end{array}\right]}\) \(\newcommand{\fivevec}[5]{\left[\begin{array}{r}#1 \\ #2 \\ #3 \\ #4 \\ #5 \\ \end{array}\right]}\) \(\newcommand{\cfivevec}[5]{\left[\begin{array}{c}#1 \\ #2 \\ #3 \\ #4 \\ #5 \\ \end{array}\right]}\) \(\newcommand{\mattwo}[4]{\left[\begin{array}{rr}#1 \amp #2 \\ #3 \amp #4 \\ \end{array}\right]}\) \(\newcommand{\laspan}[1]{\text{Span}\{#1\}}\) \(\newcommand{\bcal}{\cal B}\) \(\newcommand{\ccal}{\cal C}\) \(\newcommand{\scal}{\cal S}\) \(\newcommand{\wcal}{\cal W}\) \(\newcommand{\ecal}{\cal E}\) \(\newcommand{\coords}[2]{\left\{#1\right\}_{#2}}\) \(\newcommand{\gray}[1]{\color{gray}{#1}}\) \(\newcommand{\lgray}[1]{\color{lightgray}{#1}}\) \(\newcommand{\rank}{\operatorname{rank}}\) \(\newcommand{\row}{\text{Row}}\) \(\newcommand{\col}{\text{Col}}\) \(\renewcommand{\row}{\text{Row}}\) \(\newcommand{\nul}{\text{Nul}}\) \(\newcommand{\var}{\text{Var}}\) \(\newcommand{\corr}{\text{corr}}\) \(\newcommand{\len}[1]{\left|#1\right|}\) \(\newcommand{\bbar}{\overline{\bvec}}\) \(\newcommand{\bhat}{\widehat{\bvec}}\) \(\newcommand{\bperp}{\bvec^\perp}\) \(\newcommand{\xhat}{\widehat{\xvec}}\) \(\newcommand{\vhat}{\widehat{\vvec}}\) \(\newcommand{\uhat}{\widehat{\uvec}}\) \(\newcommand{\what}{\widehat{\wvec}}\) \(\newcommand{\Sighat}{\widehat{\Sigma}}\) \(\newcommand{\lt}{<}\) \(\newcommand{\gt}{>}\) \(\newcommand{\amp}{&}\) \(\definecolor{fillinmathshade}{gray}{0.9}\)Reaction Rates to Medical Breakthroughs: The Kinetics Legacy of Maud Menten
Figure \(\PageIndex{1}\): A graphic with basic facts about Maud Menten, co-inventor of the Michaelis-Menten equation. Reproduced with permission from Smithsonian Institution Archives, Accession 90-105, Science Service Records, Image No. SIA2008-5999.
Chemical reactions happen all around us, from metabolic pathways in living organisms to large-scale materials synthesis and drug discovery. Why do some reactions occur in seconds, while others take years? How can we control the rate at which they happen? These questions lie at the heart of chemical kinetics, the study of reaction rates.
One of the most influential scientists in this field was Maud Menten, a Canadian researcher and University of Toronto alumna. Menten earned her bachelor’s, master’s, and M.D. from U of T, making her one of the first Canadian women to qualify as a medical doctor. At a time when research opportunities for women in Canada were limited, she travelled to Germany to continue her scientific career. There, she collaborated with Leonor Michaelis to tackle a question that puzzled scientists: how do enzymes, the biological catalysts that power life, actually work?
Before Menten’s work, little was known about how enzymes control reactions inside living organisms. Menten and Michaelis helped develop a model showing how enzymes bind to specific targets and speed up reactions. They were able to quantify how the rate of an enzyme-catalyzed reaction depends on substrate concentration, describing this mathematical relationship with the Michaelis-Menten equation.
Figure \(\PageIndex{2}\): An illustration of the function of an enzyme. The enzyme binds its substrate, where a reaction occurs to transform it into product(s), which are subsequently released from the enzyme. Reproduced with permission from Wikimedia Commons under Creative Commons license CC-BY.
Today, more than a century later, Michaelis-Menten kinetics are still taught in science classrooms worldwide. Parameters from the Michaelis-Menten equation have become standard measures in the characterization of enzyme activity. Over time, this work has been applied beyond enzymes to other important biological interactions, such as antigen-antibody binding, DNA hybridization, and drug-target interactions. Maud Menten’s breakthroughs not only advanced biological chemistry but also influenced medicine and industry. In this chapter, you’ll learn the fundamentals of chemical kinetics: what reaction rates are, the factors that affect them, how they’re measured, and how chemists use this knowledge to speed up reactions and control chemical processes.
Sources:
- Le, H.; Algaze, S.; Tan, E. Michaelis-Menten Kinetics. Chemistry LibreTexts. https://chem.libretexts.org/Bookshelves/Biological_Chemistry/Supplemental_Modules_(Biological_Chemistry)/Enzymes/Enzymatic_Kinetics/Michaelis-Menten_Kinetics.
- Srinivasan, B. A Guide to the Michaelis–Menten Equation: Steady State and Beyond. The FEBS Journal 2022, 289 (20), 6086–6098. https://doi.org/10.1111/febs.16124.
- Leonor Michaelis and Maud Leonora Menten. Science History Institute. https://www.sciencehistory.org/education/scientific-biographies/leonor-michaelis-and-maud-leonora-menten/.
- Maud L. Menten, MD PhD | CMHF. https://www.cdnmedhall.ca/laureates/maudmenten.