Abstract
The covalent attachment of heme to apocytochrome c, which is catalyzed by the mitochondrial enzyme cytochrome c heme lyase, was dependent on NADH. In addition, a cofactor present in reticulocyte lysate or a Neurospora crassa cytosol fraction was required for the NADH-dependent step. In the absence of NADH, apocytochrome c was bound to the mitochondrial surface and remained accessible to externally added proteases. In the presence of NADH, covalent attachment of heme occurred with concomitant translocation of cytochrome c across the outer mitochondrial membrane to a protease-resistant location. Both heme attachment and translocation were inhibited by the heme analogue deuterohemin.
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