Mutations in the heme b-binding residue of SDHC inhibit assembly of respiratory chain complex II in mammalian cells.
Respiratory chain complex II has been extensively studied but little is known about its assembly and the role of its heme group. Mutations in the phylogenetically conserved histidine 127 of the SDHC subunit have been shown to abrogate heme binding in yeast and bacteria without impairing complex II assembly or enzymatic activities. Here we show that in mammalian cells these mutations lead to a complete reduction of SDHC in mitochondria, a destabilisation of SDHD and SDHB, and to an abrogation of complex II enzymatic activities, suggesting that in mammalian cells complex II assembly is more complex than in lower organisms.
Lemarie
Anthony
A
Imperial College London, Department of Experimental Medicine and Toxicology, Division of Investigative Science, Du Cane Road, London W12 0NN, UK.
Grimm
Stefan
S