Selective oxidation of non-activated carbon atoms still remains an unsolved issue in synthetic chemistry. The major object of this thesis was to detect and optimize enzymes, which selectively hydroxylate the linear alkane n-octane, preferably in the subterminal position(s). The important chiral intermediates such as (R)- or (S)-2-octanol are widely used as a raw material in industry for the production of esters, pharmaceutical, cosmetics, and food additives. Since cytochrome P450 monooxygenases (CYPs) have the ability to introduce molecular oxygen intro vast variety of organic molecules, they were applied as biocatalysts. The second oxygen atom is reduced to water. The electrons which are required for this reaction are derived from the cofactors (mostly NADH or NADPH) and transferred to the heme iron of CYPs via electron transfer proteins. Another theme of this thesis dealt with the enzymatic hydroxylation of the oil occurring cycloalkanes C8, C10 and C12. The incorporated P450 systems have their origin in prokaryotic (B. megaterium) and eukaryotic (C. apicola) organisms. In the final chapter of the dissertation the immobilization of a P450 monooxygenase heme domain on different mesoporous silicates was investigated. Within this work the best characterized and widely applied P450 enzyme CYP102A1 from B.
megaterium, also known as P450 BM-3,
د محمد محمود محمد عبد الفتاح | DR MOHAMMAD MAHMOUD MOHAMMAD ADEL FATAH | 9980