Cytochrome P450 and biological hydroxylation reactions.
Cytochrome P450 and biological hydroxylation reactions.
复制标题
细胞色素 P450 和生物羟基化反应。
DOI:
10.1007/bfb0019663
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发表时间:
1979
影响因子:
8.6
通讯作者:
V. Ullrich
中科院分区:
文献类型:
--
作者:
V. Ullrich
The essential role of molecular oxygen, now termed dioxygen, as an energy providing source in aerobic living systems has always been evident but the mechanism by which this energy is used to drive biological oxidations has been controversial for many years. In the mid 1930" s O. Warburg 1) concluded from model studies of ironcatalyzed oxidations with molecular oxygen that an activation of the dioxygen molecule was the crucial event for biological oxidations, which at that. time were still rather ill defined and thought mainly to consist of glycolysis and mitochondrial respiration. In contrast, H. Wieland 2) was the proponent of the dehydrogenation hypothesis which considered the oxygen molecule merely as an electron sink for substrate hydrogen. It was this mechanism which proved to be correct for all energy producing reactions in the cell. Warburg's idea of oxygen activation was almost forgotten until in 1955 Mason 3) and Hayaishi 4) demonstrated, using the stable isotope 1802, that biological oxidations which proceed by a direct incorporation of dioxygen into organic compounds are rather common in nature. These findings initiated a boom in the research on the corresponding enzymic reactions. It is now established that these oxygenations are catalyzed by a variety of dioxygen activating enzymes, which were designated" oxygenases" by Hayaishi s). Depending on whether both oxygen atoms or only one atom are introduced into the substrate, a subclassification into" dioxygenases" and" monooxygenases" was proposed and the following stoichiometry established: