In biochemistry, lipoic acid (lipoamide) functions as a swinging-arm cofactor in multienzyme dehydrogenase complexes. It serves as a cofactor for which enzyme system(s)?

Introduction / Context:
Lipoic acid (often attached to proteins as lipoamide) is a classic cofactor in oxidative decarboxylation reactions of central metabolism. Knowing which enzyme complexes require lipoic acid helps connect carbohydrate oxidation to the citric acid cycle.

Given Data / Assumptions:

• Lipoic acid participates in acyl-group transfer and redox chemistry.
• Multienzyme complexes use swinging prosthetic arms to channel intermediates efficiently.
• We are comparing dehydrogenase complexes in core metabolism.

Concept / Approach:
Lipoic acid is covalently linked to a lysine on the E2 subunit (dihydrolipoyl transacetylase or transsuccinylase) of 2-oxoacid dehydrogenase complexes. It accepts an acyl group from the decarboxylated 2-oxoacid and is then reoxidized, coupling acyl transfer to NADH production.

Step-by-Step Solution:
Identify complexes using lipoamide: pyruvate dehydrogenase (PDH) and α-ketoglutarate dehydrogenase (OGDH).Recall shared architecture: E1 (decarboxylase, TPP-dependent), E2 (lipoamide arm), E3 (dihydrolipoamide dehydrogenase, FAD-dependent).Conclude that both PDH and OGDH require lipoic acid as an essential cofactor.Di-hydroorotate dehydrogenase is a different enzyme (pyrimidine biosynthesis) and does not use lipoic acid.

Verification / Alternative check:
Standard biochemistry texts describe identical lipoamide-centered mechanisms for PDH and OGDH, and similarly for branched-chain α-ketoacid dehydrogenase.

Why Other Options Are Wrong:

• Pyruvic dehydrogenase or α-ketoglutaric dehydrogenase alone are incomplete; both use lipoamide.
• Di-hydroorotate dehydrogenase uses flavins and quinones, not lipoic acid.

Common Pitfalls:
Confusing lipoic acid (E2 cofactor) with thiamine pyrophosphate (E1 cofactor) or FAD/NAD+ (E3 cofactor). Each plays a distinct role.

Final Answer:
both (a) and (b)