The idea in this group transfer reaction is to have the -OH group on the C6 alcohol carbon of glucose to "attack" the terminal phosphate of ATP.

-OH is not a good attacking agent for a group transfer reaction- it would be much better if it were unprotonated -O- instead.

  1. Both substrates (Glucose and ATP) must be in the active site at the same time.
  2. The first step in the catalysis after both substrates have bound to the active site involves "base catalysis". An amino acid side chain (Asparate in the case of hexokinase) helps to remove a proton from the -OH to generate the required -O- and the protonated Aspartic Acid.
  3. The -O- attacks the terminal phosphate.
  4. This causes "too many bonds" to phosphate so one pair of electrons must exit - these end up as a minus charge on what used to be the "middle" phosphate of ATP.

The results are shown. The H from the -OH group on C6 is now on the amino acid side chain. The phosphate group has been transferred to the alcohol carbon of glucose and ADP is the other product.

Aerobic Glucose Metabolism

NADH Dehydrogenase


Enzyme Name

NADH Dehydrogenase


Reaction Catalyzed

REDOX

Reaction Type

Oxidation Reduction

Pathway Involvement

Oxidative Phosphorylation

Cofactors/Cosubstrates

cofactors
  • FMN - Flavin MonoNucleotide
  • several iron sulfur clusters
cosubstrate: Coenzyme Q