Answer:
1. Pyruvate reacts with TPP and is decarboxylated forming hydroxyethyl-TPP.
2. The lipoamide arm of E2 moves to the active site of E1, enabling the transfer of the acetyl group to the lipoamide.
3. The acetyl lipoamide arm of E2 moves to the active site of E2, where the acetyl group is transferred to CoA, forming acetyl-CoA and the reduced form of lipoamide.
4. The lipoamide arm moves to the active site of E3 where the reduced lipoamide is oxidized by FAD forming the active lipoamide and FADH2.
5. FADH2 is reoxidized to FAD reducing NAD+ to NADH.
Explanation:
The oxidation of pyruvate to AcetylCoA is catalyzed by the pyruvate dehydrogenase complex. The reaction is an irreversible oxidative decarboxylation process in which the carboxyl group of pyruvate is removed as a molecule of carbon dioxide, CO₂, while the remaining two carbons are attached to a CoASH molecule to form acetylCoA.
The pyruvate dehydrogenase complex contains three enzymes - Pyruvate dehydrogenase known as E₁, dihydrolipoyl transacetylase known as E₂, and dihydrolipoyl dehydrogenase known as E₃. It also requires five coenzymes namely: thiamine pyrophosphate (TPP), flavine adenine dinucleotide (NAD), coenzyme A (CoA-SH), nicotinamide adenine dinucleotide (NAD) and lipoate.
Oxidative decorbyxylation of pyruvate takes place in the pyruvate dehydrogenase complex in five steps:
1. Pyruvate reacts with TPP and is decarboxylated forming hydroxyethyl-TPP.
2. The lipoamide arm of E2 moves to the active site of E1, enabling the transfer of the acetyl group to the lipoamide.
3. The acetyl lipoamide arm of E2 moves to the active site of E2, where the acetyl group is transferred to CoA, forming acetyl-CoA and the reduced form of lipoamide.
4. The lipoamide arm moves to the active site of E3 where the reduced lipoamide is oxidized by FAD forming the active lipoamide and FADH2.
5. FADH2 is reoxidized to FAD reducing NAD+ to NADH.
