Abstract
The influence of singlet oxygen (1O2), generated by red light irradiation of oxygenated suspensions containing aluminium phthalocyanine sulphonate, on the membrane bound enzyme β‐hydroxybutyrate dehydrogenase was investigated. The inactivation rates were measured using a spectrophotometry assay which involves disruption of the mitochondria. A novel NMR assay was also used to measure the activity of the enzyme in intact mitochondria. Relatively high inactivation rates of around 109M−1 s−1 were observed in H2O buffer, and rates in D2O were a factor of 1.7 faster. Significant differences in enzyme inactivation rates by 1O2 were observed, not only between disrupted and intact mitochondria but also between the NMR assay results and the spectrophotometric assay results. The results indicate the value of a specific assay which does not require the disruption of the biological system.
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