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Function and regulation of cytochrome P-450 in alkane-assimilating yeast

I. Selective inhibition with carbon monoxide in growing cells

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Abstract

A method for selective and reversible inhibition of the alkane hydroxylating cytochrome P-450 in growing yeast cells was developed. Using low concentrations of carbon monoxide in a specially adapted small-scale fermentor system a complete inhibition of the first step of alkane degradation was obtained, obviously without influencing further metabolic steps. Thus, fatty alcohols which were shown to be the immediate products of the cytochrome P-450 catalyzed reaction were utilized with unchanged rates by yeast cultures blocked with carbon monoxide in alkane degradation.

Moreover, significant differences were found in the pO2-dependencies of utilization of n-alkanes, fatty alcohols and further intermediates. It was concluded, that the alkane hydroxylating cytochrome P-450 system is distinguished by the lowest oxygen affinity among the oxygen-activating enzyme systems involved in alkane assimilation.

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Abbreviations

cyt:

cytochrome

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Schunck, W.H., Mauersberger, S., Huth, J. et al. Function and regulation of cytochrome P-450 in alkane-assimilating yeast. Arch. Microbiol. 147, 240–244 (1987). https://doi.org/10.1007/BF00463482

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  • DOI: https://doi.org/10.1007/BF00463482

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