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When enzymes interact with substrates (i.e. a small ADP molecule and the much larger ATP synthase), does quantum mechanics play a significant role? Or can the interactions be relatively accurately be understood using simply classical mechanics principles?

For example, considering a free body diagram when I insert a key into a lock, the interactions between the key and the lock can be accurately modeled using simply classical mechanics (such as friction, normal forces, etc).

However, since the scale of proteins and molecules are much smaller, could the binding of ADP to ATP synthase still be accurately modeled using classical mechanics (i.e. electrostatic forces, physical contact forces, etc.)? Or are quantum principles very significant?

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  • $\begingroup$ Related. $\endgroup$ – canadianer Oct 14 at 9:14
  • $\begingroup$ I think, this paper can help you understand current state of Quantum Biology and related issues. $\endgroup$ – Dexter Oct 14 at 12:20
  • $\begingroup$ In the main, I think quantum mechanics has not entered the world of enzyme kinetics. However, one important exception is in hydrogen transfer reactions and isotope effects, where quantum-mechanical 'tunneling' has been unequivocally established. Any paper by Judith Klinman on this subject is well worth reading, including Hydrogen tunneling in enzyme reactions $\endgroup$ – user1136 Oct 14 at 15:01
  • $\begingroup$ A pdf of the Klinman Science paper may be found here. Formerly an interest, but your (great) question 'a bit too big' for me at the moment (but I'll have a go if no-one else does, although not in the short-term) $\endgroup$ – user1136 Oct 14 at 15:03
  • $\begingroup$ Another great paper by the aforementioned Professor Klinman : Hydrogen tunneling in biology (Kohen & Klinman) $\endgroup$ – user1136 Oct 14 at 15:13

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