Why catalysts affect forward and reverse reactions?

AI Thread Summary
Enzymes facilitate both forward and reverse reactions due to their specific shapes, which allow them to bind with substrates in both states. The discussion highlights a common confusion stemming from simplified biological diagrams that typically illustrate only the forward reaction. It is clarified that the enzyme-substrate interaction forms an intermediate complex, enabling the reaction to proceed in either direction, although thermodynamics often favor one direction. Additionally, the effectiveness of catalysts, including enzymes compared to artificial ones, can be measured using metrics like Turn Over Number and the number of moles of product per unit mass. The conversation emphasizes the continuous nature of enzyme activity, suggesting that enzymes can accommodate both reactants and products due to their adaptable shapes.
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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