Enzyme Confusion: Lowering Activ. Energy & Bond Strain

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Discussion Overview

The discussion revolves around the mechanisms by which enzymes lower activation energy in chemical reactions, including the role of transition states and bond strain. Participants explore theoretical aspects of enzyme catalysis, addressing both conceptual and technical elements of enzymatic action.

Discussion Character

  • Exploratory
  • Technical explanation
  • Conceptual clarification

Main Points Raised

  • One participant expresses confusion about how enzymes lower activation energy, questioning if the enzyme-substrate transition state is a lower energy state than the substrate state.
  • Another participant challenges the terminology used, specifically the term "substrate1-substrate2 state," suggesting it may not be accurate.
  • A participant clarifies their reference to the transition state with and without the enzyme, indicating that diagrams helped clarify their understanding.
  • One participant explains that enzymes lower activation energy by stabilizing the transition state or allowing the reaction to occur through a different transition state, noting that the specifics depend on the enzyme.
  • Concerns are raised about the concept of bond strain, questioning how an enzyme can apply strain without contributing energy, and where that energy would come from.
  • A later reply suggests that the interaction between an enzyme and its substrate is generally exergonic, releasing free energy that can be utilized to induce strain on the substrate, using a metaphor involving magnets and a rubber band to illustrate the concept.

Areas of Agreement / Disagreement

Participants exhibit some disagreement regarding terminology and the specifics of enzyme action. While there are shared understandings of the general mechanisms, the discussion remains unresolved on certain points, particularly concerning the energy dynamics involved in bond strain.

Contextual Notes

Participants express uncertainty about specific terms and concepts, indicating a need for clearer definitions and examples. The discussion includes various assumptions about the nature of enzyme-substrate interactions and the thermodynamic principles involved.

ifihadsomebacon
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So, I know that enzymes are not consumed in the reactions they catalyze, and that they catalyze these reactions by lowering the activation energy. So, in an uncatalyzed reaction, more energy is required to "kick off" the reaction, resulting in the same overall change in free energy. I'm just sort of confused as to how this happens, is the enzyme-substrate1-substrate2 transition state just a lower energy state than the substrate1-substrate2 state?

Also, I read in my Biology textbook that bond strain was one of the ways that enzymes can catalyze a reaction, but enzymes don't contribute any energy. Doesn't the enzyme putting physical strain on a substrate require energy? Where does that come from?
 
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Borek said:
Not sure what you mean by substrate1-substrate2 state, I feel like you are making that up.

Have you seen diagrams like this one: https://en.wikipedia.org/wiki/Enzyme#/media/File:Enzyme_catalysis_energy_levels_2.svg

I guess I was just trying to refer to the transition state with the enzyme vs. the transition state without the enzyme, sorry if I was unclear. But thank you, that diagram actually helped a lot, all of the ones in my biology textbook are a lot more basic.
 
ifihadsomebacon said:
So, I know that enzymes are not consumed in the reactions they catalyze, and that they catalyze these reactions by lowering the activation energy. So, in an uncatalyzed reaction, more energy is required to "kick off" the reaction, resulting in the same overall change in free energy. I'm just sort of confused as to how this happens, is the enzyme-substrate1-substrate2 transition state just a lower energy state than the substrate1-substrate2 state?

There are many ways that an enzyme can lower the activation energy of a chemical reaction. Almost always, this occurs by lowering the energy of the transition state. This could occur by stabilizing the transition state through interactions of the transition state with the enzyme or it could occur by allowing the reaction to occur through a different transition state than the uncatalyzed reaction. The exact details of how the enzyme does this will depend on the enzyme being studied.

Also, I read in my Biology textbook that bond strain was one of the ways that enzymes can catalyze a reaction, but enzymes don't contribute any energy. Doesn't the enzyme putting physical strain on a substrate require energy? Where does that come from?

In general, the interaction between an enzyme and its substrate is a thermodynamically favorable (exergonic) process that results in a release of free energy. Sometimes, this free energy of binding can be used for purposes such as putting strain on a molecule to promote catalysis. Imagine putting two magnets on either side of a wall that is 5 ft apart (an enzyme active site with sites that interact with different parts of the substrate). Now imagine a 4 ft rubber band with magnets attached on either side (the substrate). If the magnets are strong enough, binding of the magnets on the rubber band to the magnets on the wall can stretch the rubber band and put strain on it. Similarly, strong binding interactions of the enzyme with one part of the substrate can allow the enzyme to force another part of the substrate to adopt a strained conformation.
 
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