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. 2021 Sep 30;26(3):138–148. doi: 10.6065/apem.2142154.077

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© 2021 Annals of Pediatric Endocrinology & Metabolism

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Fig. 1. — Diagram of type 1 (mitochondrial) P450 enzymes. The inner mitochondrial membrane is indicated by the hatched area; both ferredoxin reductase (FeRed) and the P450 are membrane bound, but ferredoxin (Fedx) is not. NADPH donates a pair of electrons to the flavin adenine dinucleotide (FAD) moiety of ferredoxin reductase; which then donates them to the 2Fe2S center of ferredoxin (depicted by the ball-and-stick image). The same surface of the ferredoxin molecule interacts with both the FAD of ferredoxin reductase and the redox partner binding site of the P450 by electrostatic (charge-charge) interactions. Ferredoxin thus acts as an indiscriminate electron-shuttling protein that can support the catalysis of any available type 1 P450. The electrons reach the heme iron of the P450 permitting catalysis. NADP+, nicotinamide adenine dinucleotide phosphate NADPH, reduced adenine dinucleotide phosphate.