Institute for Microbial and Biochemical Technology, Forest Products Laboratory, U.S. Department of Agriculture, Madison, Wisconsin 53705.
Appl Environ Microbiol. 1994 Jun;60(6):1956-61. doi: 10.1128/aem.60.6.1956-1961.1994.
The manganese peroxidase (MnP) of Phanerochaete chrysosporium supported Mn(II)-dependent, H(2)O(2)-independent lipid peroxidation, as shown by two findings: linolenic acid was peroxidized to give products that reacted with thiobarbituric acid, and linoleic acid was peroxidized to give hexanal. MnP also supported the slow oxidation of phenanthrene to 2,2'-diphenic acid in a reaction that required Mn(II), oxygen, and unsaturated lipids. Phenanthrene oxidation to diphenic acid by intact cultures of P. chrysosporium occurred to the same extent that oxidation in vitro did and was stimulated by Mn. These results support a role for MnP-mediated lipid peroxidation in phenanthrene oxidation by P. chrysosporium.
白腐真菌(Phanerochaete chrysosporium)的锰过氧化物酶(MnP)支持 Mn(II)依赖、H(2)O(2)独立的脂类过氧化,这表现在两个发现中:亚麻酸被过氧化生成与硫代巴比妥酸反应的产物,亚油酸被过氧化生成己醛。MnP 还支持在需要 Mn(II)、氧和不饱和脂质的反应中,缓慢氧化菲到 2,2'-联苯酚二酸。完整的白腐真菌(P. chrysosporium)培养物将菲氧化为联苯酚二酸的程度与体外氧化的程度相同,并且 Mn 可以刺激这种氧化。这些结果支持 MnP 介导的脂类过氧化在白腐真菌(P. chrysosporium)氧化菲中的作用。