Enzymatic Oxidation of Disulfides and Thiolsulfinates by both Rabbit Liver Microsomes and a Reconstituted System with Purified Cytochrome P-450
- 1 April 1978
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 83 (4) , 1019-1027
- https://doi.org/10.1093/oxfordjournals.jbchem.a131990
Abstract
Both rabbit liver microsomes and reconstituted system with purified cytochrome P-450 and cofactors enzymatically oxidized o-dithiane (1, 2-dithiane), 3-methyl-o-dithiane, thiane and 2-methylthiane to the corresponding mono-oxygenated products; sulfides or disulfides were oxidized to the corresponding sulfoxides or thiolsulfinates, while thiolsulfinate was oxidized to thiolsulfonate. The reconstituted systems required oxygen and NADPH and were not affected by the catalase which decomposes H2O2, or by 1, 4-diazabicyclo-[2, 2, 2]octane (DABCO), which is a good quencher of singlet oxygen. The differences in the binding of substrates such as sulfides and disulfides with the enzyme system are discussed in connection with differences in the spectra of the substrates in the reconstituted system with pure cytochrome P-450. A correlation was found between the rates of oxidation of the substrates and the rates of oxidation of NADPH.Keywords
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