Functional mapping reveals the importance of yeast cytochrome b C-terminal region in assembly and function of the bc1 complex.

Genetic and molecular analyses have been undertaken for four respiratory deficient mutants (mit-). The four mutations affect the C-terminal region of apocytochrome b. The frameshift (L263STOP) and non-sense (Q338STOP) mutations give rise to a truncated apocytochrome b. The mutant G337R conserves only 32% of its NADH oxidase activity which suggests that the presence of a positively charged amino acid in the transmembranous helix 7 of cytochrome b alters, either directly or indirectly, the bc1 function, without affecting its assembly. The mutation G352V has a 65% loss of cytochrome b spectral content and prevents all of the mitochondrial respiratory activity. This leads us to believe that the glycine, conserved in position 352, may play a crucial role in bc1 complex function.