IS CELLOBIOSE OXIDASE FROM PHANEROCHAETE-CHRYSOSPORIUM A ONE-ELECTRON REDUCTASE

IS CELLOBIOSE OXIDASE FROM PHANEROCHAETE-CHRYSOSPORIUM A ONE-ELECTRON REDUCTASE
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DOI:
10.1016/0005-2728(93)90171-b
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发表时间:
1993-09-13
期刊:
BIOCHIMICA ET BIOPHYSICA ACTA
影响因子:
--
通讯作者:
PETTERSSON, G
PETTERSSON, G
中科院分区:
其他
文献类型:
--
作者:
HENRIKSSON, G;JOHANSSON, G;PETTERSSON, G

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黄孢原毛平革菌纤维二糖氧化酶(CBO)的血红素结构域增加了电子转移到单电子受体的速率。这一结论是通过比较完整的CBO、FAD片段和CBO与氰化物灭活的血红素对3,5-叔丁基-邻苯醌、三碘离子、细胞色素c和铁氰化物的还原速率得出的。纤维二糖的氧化产生过氧化氢,但该酶通过还原产物或通过与过氧化物酶直接相互作用来干扰基于过氧化物酶的测定。CBO还可以在纤维二糖存在下降解过氧化氢。CBO能迅速还原1,2,4,5-四甲氧基苯阳离子自由基。
The heme domain of cellobiose oxidase (CBO) from Phanerochaete chrysosporium increases the rate of electron transfer to one-electron acceptors. This conclusion was drawn from comparisons of the rates of reduction of 3,5-t-butyl-o-benzoquinone, triiodide ion, cytochrome c and ferricyanide by intact CBO, FAD fragment and CBO with the heme inactivated by cyanide. The oxidation of cellobiose produced hydrogen peroxide, but the enzyme disturbs peroxidase-based assays by reduction of the product or by direct interaction with the peroxidase. CBO can also degrade hydrogen peroxide in the presence of cellobiose. The 1,2,4,5-tetramethoxybenzene cation radical was rapidly reduced by CBO.