13 Facts About Complex I

Complex I is the first enzyme of the mitochondrial electron transport chain.

Complex I is the largest and most complicated enzyme of the electron transport chain.

Escherichia coli complex I is capable of proton translocation in the same direction to the established ??, showing that in the tested conditions, the coupling ion is H Na transport in the opposite direction was observed, and although Na was not necessary for the catalytic or proton transport activities, its presence increased the latter.

Possibly, the E coli complex I has two energy coupling sites, as observed for the Rhodothermus marinus complex I, whereas the coupling mechanism of the P denitrificans enzyme is completely Na independent.

Complex I contains a ubiquinone binding pocket at the interface of the 49-kDa and PSST subunits.

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Rolliniastatin-2, an acetogenin, is the first complex I inhibitor found that does not share the same binding site as rotenone.

Complex I is blocked by adenosine diphosphate ribose – a reversible competitive inhibitor of NADH oxidation – by binding to the enzyme at the nucleotide binding site.

Inhibition of complex I has been implicated in hepatotoxicity associated with a variety of drugs, for instance flutamide and nefazodone.

The inactive, but not the active form of complex I was susceptible to inhibition by nitrosothiols and peroxynitrite.

Recent investigations suggest that complex I is a potent source of reactive oxygen species.

Complex I can produce superoxide, through at least two different pathways.

Reverse electron transfer, the process by which electrons from the reduced ubiquinol pool pass through complex I to reduce NAD to NADH, driven by the inner mitochondrial membrane potential electric potential.

Point mutations in various complex I subunits derived from mitochondrial DNA can result in Leber's Hereditary Optic Neuropathy.