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Subcellular organization of alkane oxidation in the yeast Candida maltosa
Author(s) -
Mauersberger S.,
Kärgel E.,
Matyashova R. N.,
Müller H.G.
Publication year - 1987
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.3620271005
Subject(s) - biochemistry , microsome , peroxisome , cytochrome , endoplasmic reticulum , yeast , cell fractionation , chemistry , biology , membrane , enzyme , gene
After spheroplast lysis and differential centrifugation the alkane monooxygenase system consisting of cytochrome P‐450 and the NADPH‐cytochrome P‐450 reductase of alkane‐grown Candida maltosa cells is enriched in the microsomal fraction. This membrane fraction is nearly free of intact mitochondria (cytochrome oxidase) and peroxisomes (catalase), but contains considerable amounts of plasma membrane fractures (azide insensitive, vanadate‐sensitive Mg 2+ ‐ATPase) as demonstrated by biochemical an electron microscopic examinations. By means of sucrose density gradient centrifugation it was possible to separate the cytochrome P‐450 containing membranes ( = 1,11 g/cm 3 ) from the plasma membranes ( = 1,18 g/cm 3 ). Therefore the cytochrome P‐450 alkane monooxygenase system is most likely localized in the endoplasmic reticulum of the yeast cells. For the following enzymatic steps of terminal alkane oxidation to the corresponding fatty acid a quite different subcellular distribution was observed. The fatty alcohol oxidase and aldehyde dehydrogenase activities are mainly localized in the mitochondrial peroxisomal membrane fraction. During the oxidation of n‐alkanes by yeast cells the fatty alcohol should be regarded as an intracellular transport from between the cytochrome P‐450 containing endoplasmic reticulum and the sites of its further oxidation in peroxisomes and mitochondria.