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Enzymes: Transition state stabilisation + free energy?

I'm probably missing a fundamental principle but here's my problem:

So I'm studying acid-base catalysis, covalent catalysis etc. I know that they work by stabilizing the transition state by reducing charge build up e.g. O- atom on a molecule can be stabilized by proton donation.

This apparently lowers the free energy of the transition state - but why? Why does this lower the free energy of activation? Just because it's an unstable molecule, so stabilizing it is more energetically favourable? Although I don''t really understand why it's energetically favourable...

Maybe someone could point me in the direction of a topic I should read to understand this?
Hi there,

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