Williams P G, Stewart P R
Arch Microbiol. 1976 Feb;107(1):63-70. doi: 10.1007/BF00427868.
Cytochemical and ultrastructural analysis of wild-type cells of Saccharomyces cerevisiae, grown aerobically in a glucose-limited chemostat, shows that cytochrome c peroxidase is localized between the membranes of the cristae, that is, in the intracristal space. This enzyme is thus positioned appropriately within the organelle to act as an alternate terminal oxidase for the respiratory chain. The proximity of the peroxidase to major sites of generation of its two substrates may account for the small leakage of hydrogen peroxide from yeast mitochondria, as compared with the larger outflow from mammalian mitochondria. In the cytoplasmic petite mutant, gross distortion of promitochondrial membrane arrangement is evident. Nevertheless, cytochrome c perioxidase activity is present in the same amounts as is found in wild-type cells, and is localized predominantly within annuli of membrane which constitute the promitochondria in these cells. No unequivocal evidence was obtained for the localization of catalase in microbodies or other organelles in either wild-type or petite cells.
对在葡萄糖受限的恒化器中好氧生长的酿酒酵母野生型细胞进行细胞化学和超微结构分析表明,细胞色素c过氧化物酶定位于嵴膜之间,即嵴内空间。因此,这种酶在细胞器内的定位适当,可作为呼吸链的替代末端氧化酶。与哺乳动物线粒体中较大的过氧化氢流出量相比,过氧化物酶与其两种底物的主要生成位点接近,这可能是酵母线粒体中过氧化氢泄漏较少的原因。在细胞质小菌落突变体中,前线粒体膜排列明显严重扭曲。然而,细胞色素c过氧化物酶活性的含量与野生型细胞中的相同,并且主要定位于构成这些细胞前线粒体的膜环内。无论是野生型细胞还是小菌落细胞,均未获得过氧化氢酶定位于微体或其他细胞器的确切证据。