Why is the formation of an enzyme-substrate complex endergonic (induced fit model)?

Question

In the section about the induced fit model for enzyme substrate binding, my MCAT textbook claims that "The substrate has induced a change in the shape of the enzyme. This interaction requires energy, and therefore, this part of the reaction is endergonic."

As a chemist, I am a bit confused here because induced fit suggests that some kind of bonding must be happening between the enzyme and substrate (hydrogen, ionic, covalent, etc) that would induce a change in structure of both enzyme and substrate. Any kind of bond formation is STRICTLY enthalpically exothermic, so why is the formation of an enzyme-substrate complex endergonic?

Am I missing an entropic component here? Or is my assumption wrong, regarding how the induced fit chemistry operates?

I would assume that it would TAKE energy to then cleave/break all the bonds that induced structural change and release the catalyzed substrate...

Answer 1

Most reactions require an activation energy to cross an energy barrier (this you may already know) after which the reaction is downhill. Even though enzyme catalysed reactions have a relatively lower activation energy compared to that of an uncatalysed reaction, there is still a transition state that has a higher free energy compared to the products. This transition state corresponds to the enzyme-substrate complex.

               
            _{Image Source: https://en.wikibooks.org/wiki/Structural_Biochemistry/Enzyme/Activation_energy}

Free energy has enthalpic and entropic components (ΔG=ΔH-TΔS). Even though formation of bonds may reduce the enthalpy, the locking of the substrate and enzyme in a conformation also decreases the entropy. This could lead to overall increase in free energy (See here. For more details you can refer to this book- The Enzymes: Mechanisms of Catalysis by Paul Sigman. ISBN: 0121227200).