Characterization of heme-binding properties of Paracoccus denitrificans Surf1 proteins.
作者： Achim Hannappel , Freya A. Bundschuh , Bernd Ludwig
DOI: 10.1111/J.1742-4658.2011.08101.X
关键词:
摘要: Biogenesis of cytochrome c oxidase (COX) is a highly complex process involving >30 chaperones in eukaryotes; those required for the incorporation copper and heme cofactors are also conserved bacteria. Surf1, associated with heme a insertion Leigh syndrome if defective humans, present as two homologs soil bacterium Paracoccus denitrificans, Surf1c Surf1q. In an in vitro interaction assay, transfer from purified synthase, CtaA, to was followed, both Surf proteins were tested their binding properties. Mutation four strictly amino acid residues within transmembrane part each Surf1 protein confirmed requirement binding. Interestingly mutation tryptophan residue helix II (W200 W209 Surf1q) led drastic switch composition, now being populated mostly by heme o, intermediate biosynthetic pathway. This discriminates between moieties, apparently coordinates formyl group heme a, most likely presents cofactor spatial orientation suitable optimal its target site subunit I cytochrome c oxidase.
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