Abstract Energy is a crosscutting concept in science, but college students often perceive a mismatch between how their biology and chemistry courses discuss the topic. The challenge of reconciling these disciplinary differences can promote faulty reasoning—for example, biology students often develop the incorrect idea that breaking bonds is exothermic and releases energy. We hypothesize that one source of this perceived mismatch is that biology and chemistry textbooks use different visual representations of bond breaking and formation. We analyzed figures of ATP hydrolysis from 12 college‐level introductory biology textbooks and coded each figure for its representation of energy, bond formation, and bond breaking. For comparison, we analyzed figures from six college‐level introductory chemistry textbooks. We found that the majority (70%) of biology textbook figures presented ATP hydrolysis in the form “one reactant → multiple products” and “more bonds in reactants → fewer bonds in products”. In contrast, chemistry textbook figures of the form “one reactant → multiple products” and “more bonds → fewer bonds” were predominantly endothermic reactions, which directly contradicts the exothermic nature of ATP hydrolysis. We hypothesize that these visual inconsistencies may be a contributing factor to student struggles in constructing a coherent mental model of energy and bonding.
more »
« less
This content will become publicly available on April 3, 2027
Making sense of ATP hydrolysis: how students reconcile conflicting ideas from chemistry and biology
Energy is a core concept across STEM, but disciplinary differences in how the topic is taught can lead students to develop a fragmented understanding. One well-documented misconception is that “breaking bonds releases energy,” a belief especially common when biology students reason about adenosine triphosphate (ATP) hydrolysis. Using Hammer’s resources framework, we investigated whether students’ misconceptions about exothermic bond breaking stemmed from a failure to activate chemistry knowledge in a biology context, or from a complete absence of that knowledge. We conducted semi-structured interviews in which introductory biology students first explained why ATP hydrolysis releases energy and then chose the reaction coordinate diagram that best represented the process. Initially, most students claimed that ATP hydrolysis releases energy because bonds are broken. However, when prompted with a reaction coordinate diagram, one third of students spontaneously corrected themselves, realizing that breaking bonds requires, rather than releases, energy. These results suggest that even when introductory biology students make errors in chemical reasoning, many actually possess the relevant underlying knowledge (e.g., “breaking bonds requires energy”) but fail to activate it in a biology context.
more »
« less
- Award ID(s):
- 2244099
- PAR ID:
- 10679375
- Editor(s):
- Liao, Min-Ken
- Publisher / Repository:
- Journal of Microbiology and Biology Education Research
- Date Published:
- Journal Name:
- Journal of Microbiology & Biology Education
- ISSN:
- 1935-7877
- Format(s):
- Medium: X
- Sponsoring Org:
- National Science Foundation
More Like this
-
-
A misconception among biology students is that breaking bonds in adenosine triphosphate (ATP) releases energy. This misconception may be related to imprecise representations of chemical bonding in common diagrams of ATP hydrolysis. We interviewed 33 undergraduate students and randomly assigned them to interpret a figure of ATP hydrolysis that either emphasized bond breaking in the reactants or the formation of new bonds in the products. Students who saw the figure emphasizing bond breaking were more likely to incorrectly classify ATP hydrolysis as endergonic, while students who saw the figure explicitly illustrating bond formation were more likely to use chemically-sound reasoning to describe the reaction.more » « less
-
Chemical reactions that mimic the function of ATP hydrolysis in biochemistry are of current interest in nonequilibrium systems chemistry. The formation of transient bonds from these reactions can drive molecular machines or generate materials with time-dependent properties. While the behavior of these systems can be complicated, the underlying chemistry is often simple: they are therefore potentially interesting topics for undergraduate introductory organic chemistry students, combining state-of-the-art advances in systems chemistry with straightforward reactions. Here, a teaching experiment has been developed that explores the transient assembly of benzoic acid derivatives driven by carbodiimide hydration. Working in teams, students examine the formation and decomposition of anhydrides from two benzoic acids using a carbodiimide “fuel”. The students examine classic reaction kinetics of anhydride hydrolysis using two independent methods, NMR and IR spectroscopies. They then explore how the amount of carbodiimide affects the lifetimes of precipitates of benzoic anhydride as a simple example of out-of-equilibrium self-assembly.more » « less
-
Kinesin motor proteins perform several essential cellular functions powered by the adenosine triphosphate (ATP) hydrolysis reaction. Several single-point mutations in the kinesin motor protein KIF5A have been implicated to hereditary spastic paraplegia disease (HSP), a lethal neurodegenerative disease in humans. In earlier studies, we have shown that a series of HSP-related mutations can impair the kinesin’s long-distance displacement or processivity by modulating the order–disorder transition of the linker connecting the heads to the coiled coil. On the other hand, the reduction of kinesin’s ATP hydrolysis reaction rate by a distal asparagine-to-serine mutation is also known to cause HSP disease. However, the molecular mechanism of the ATP hydrolysis reaction in kinesin by this distal mutation is still not fully understood. Using classical molecular dynamics simulations combined with quantum mechanics/molecular mechanics calculations, the pre-organization geometry required for optimal hydrolysis in kinesin motor bound to α/β-tubulin is determined. This optimal geometry has only a single salt-bridge (of the possible two) between Arg203-Glu236, putting a reactive water molecule at a perfect position for hydrolysis. Such geometry is also needed to create the appropriate configuration for proton translocation during ATP hydrolysis. The distal asparagine-to-serine mutation is found to disrupt this optimal geometry. Therefore, the current study along with our previous one demonstrates how two different effects on kinesin dynamics (processivity and ATP hydrolysis), caused by a different set of genotypes, can give rise to the same phenotype leading to HSP disease.more » « less
-
We present a thermodynamically consistent energetic variational model for active nematics driven by ATP hydrolysis. Extending the classical Toner–Tu framework, we introduce a chemo-mechanical coupling mechanism in which the self-advection and polarization dynamics are modulated by the ATP hydrolysis rate. The model is derived using an energetic variational approach that integrates both chemical free energy and mechanical energy into a unified energy dissipation law. The reaction rate equation explicitly incorporates mechanical feedback, revealing how active transport and alignment interactions influence chemical fluxes and vice versa. This formulation not only preserves consistency with non-equilibrium thermodynamics but also provides a transparent pathway for modeling energy transduction in active systems. We also present numerical simulations demonstrating the positive energy transduction under a specific choice of model parameters. The new modeling framework offers new insights into energy transduction and regulation mechanisms in biologically related active systems.more » « less
An official website of the United States government
