Why catalysts affect forward and reverse reactions?

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Discussion Overview

The discussion revolves around the role of enzymes as catalysts in both forward and reverse reactions, exploring why the specific shape of enzymes facilitates these processes. Participants also inquire about comparisons between organic and artificial catalysts, particularly regarding their effectiveness.

Discussion Character

  • Exploratory
  • Conceptual clarification
  • Debate/contested

Main Points Raised

  • One participant expresses confusion about how the specific shape of enzymes aids in both forward and reverse reactions, noting that simplified diagrams often only depict the forward reaction.
  • Another participant mentions that the efficiency of a catalyst can be measured by the number of moles of product per unit mass.
  • A participant outlines the general reaction mechanism involving reactants, an enzyme, an intermediate complex, and products, suggesting that the reaction can proceed in both directions but is typically favored in one due to thermodynamics.
  • One participant questions their understanding of the active site's shape and its interaction with substrates, wondering if it is possible for an enzyme to be designed to only catalyze the forward reaction.
  • Another participant states that the enzyme must accommodate both the initial and final shapes of the substrates, indicating that the change is continuous.

Areas of Agreement / Disagreement

The discussion reflects a lack of consensus on the visualization and understanding of enzyme functionality in catalyzing both forward and reverse reactions. Participants express differing levels of understanding and inquiry into the mechanisms involved.

Contextual Notes

Participants highlight potential misconceptions regarding enzyme shapes and their roles in reactions, as well as the need for clarity on the measurement of catalyst efficiency. There is an acknowledgment of the complexity of enzyme interactions that may not be fully captured in simplified educational diagrams.

Who May Find This Useful

This discussion may be useful for students and individuals interested in biochemistry, particularly those exploring enzyme functionality and catalyst comparisons.

Pharrahnox
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Based on the very basic understanding on enzymes I have gained from Year 12 Biology and Chemistry, I don't undesrtand why the enzymes specific shape also helps the reverse reaction. I guess my trouble would be due to the simplified diagrams I've seen from Biology, where only the forward reaction is shown to be catalysed.

So if anyone has any explanations or links, that would be great.

Also, a side question, does anyone have a link that compares organic and artificial catalysts; I've heard that enzymes are ridiculously more effective than standard artificial catalysts, but I can't really find what I'm looking for on the interenet. What do you compare? Is it the Turn Over Number?

Anyway, any clarification would be greatly appreciated.
 
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Pharrahnox said:
Based on the very basic understanding on enzymes I have gained from Year 12 Biology and Chemistry, I don't undesrtand why the enzymes specific shape also helps the reverse reaction. I guess my trouble would be due to the simplified diagrams I've seen from Biology, where only the forward reaction is shown to be catalysed.

So if anyone has any explanations or links, that would be great.

Also, a side question, does anyone have a link that compares organic and artificial catalysts; I've heard that enzymes are ridiculously more effective than standard artificial catalysts, but I can't really find what I'm looking for on the interenet. What do you compare? Is it the Turn Over Number?

Anyway, any clarification would be greatly appreciated.
I can't comment on the first part, but one quantity used to measure the 'efficiency' of a catalyst is the number of moles of the product per unit mass (often mmol/g).
 
In general you have:

reactant + enzyme <-> intermediate complex <-> product + enzyme

So in principle the reaction can go both ways. Typically one direction is preferred due to the thermodynamics of the process.
 
Thanks Vagn and Borek for your prompt replies.

I guess I am just incorrectly visualising the "shape" of the active site, and how it bonds with the substrate, whether that be the reactants or products of a particular reaction. It seems strange that an enzyme could not be manufactured to have a "shape" that only works for the forward reaction. Can you think of what exactly I might be missing?
 
Enzyme has to fit both the initial and the final "shape", change is continuous.
 
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Ok, that makes sense. Thanks for your help.
 

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