Cytochrome oxidase Neurospora crassa

Weiss, H., and Kolb, H. J., 1979, Isolation of mitochondrial succinate ubiquinone reductase, cytochrome c reductase and cytochrome c oxidase from Neurospora crassa using nonionic detergent, Eur. J. Biochem. 99 139nl49. 

There are no plasma membrane-bound enzymes whose activities are known to be specifically and sufficiently altered to account for growth Inhibition by the sterol inhibitors at sub-MIC doses. A likely candidate is chitin synthetase, but the activity of this enzyme is not reduced in fact, sterol inhibitor-treated fungi contain more glucosamine polymers than controls. However, the altered deposition of chitin (see above references) may reflect a discontinuity between cytoskeletal elements which are believed to be involved in cell wall formation and the plasma membrane, but it is unlikely that this is at the root of growth inhibition since a wall-less slime mutant of Neurospora crassa is as sensitive as the wild-type strain to propiconazole (57TI Cytochrome oxidase and microsomal ATPase are inhibited by high concentrations (10 5,... 

Further data were obtained by Weiss et al. (1971) with Neurospora crassa. Chromatography of mitochondrial protein labeled in vivo in the presence of cycloheximide (CH), yielded fractions containing difilerent amounts of radioactivity. The fraction of highest specific radioactivity was pure and enzymically active cytochrome oxidase. Separation of the polypeptide chains of this enzyme by SDS gel electrophoresis revealed five protein bands of which, in the presence of CH, only one polypeptide was highly labeled. Similar results were obtained with cytochrome oxidase from Locusta migratoria (Weiss et al, 1972). Here seven polypeptide chains were obtained. One, with a molecular weight of about 19,000, was labeled in the presence of CH and may be a product of mitochondrial protein synthesis. 

Biogenesis of Cytochrome Oxidase and Cytochrome b in Neurospora crassa... 

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