pH-dependent electron transfer reaction and direct bioelectrocatalysis of the quinohemoprotein pyranose dehydrogenase.
pH-dependent electron transfer reaction and direct bioelectrocatalysis of the quinohemoprotein pyranose dehydrogenase.
复制标题
pH 依赖性电子转移反应和醌血红素蛋白吡喃糖脱氢酶的直接生物电催化。
DOI:
10.1016/j.bbrc.2016.06.096
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发表时间:
2016
影响因子:
3.1
通讯作者:
N. Nakamura
中科院分区:
文献类型:
--
作者:
K. Takeda;H. Matsumura;T. Ishida;Makoto Yoshida;K. Igarashi;M. Samejima;H. Ohno;N. Nakamura
A pyranose dehydrogenase fromCoprinopsis cinerea(CcPDH) is an extracellular quinohemoeprotein, which consists ab-type cytochrome domain, a pyrroloquinoline-quinone (PQQ) domain, and a family 1-type carbohydrate-binding module. The electron transfer reaction ofCcPDH was studied using some electron acceptors and a carbon electrode at various pH levels. Phenazine methosulfate (PMS) reacted directly at the PQQ domain, whereas cytochromec(cytc) reacted via the cytochrome domain of intactCcPDH. Thus, electrons are transferred from reduced PQQ in the catalytic domain ofCcPDH to hemebin the N-terminal cytochrome domain, which acts as a built-in mediator and transfers electron to a heterogenous electron transfer protein. The optimal pH values of the PMS reduction (pH 6.5) and the cytcreduction (pH 8.5) differ. The catalytic currents for the oxidation ofl-fucose were observed within a range of pH 4.5 to 11. Bioelectrocatalysis ofCcPDH based on direct electron transfer demonstrated that the pH profile of the biocatalytic current was similar to the reduction activity of cytccharacters.
DOI:
--
发表时间:
2017
期刊:
影响因子:
--
作者:
細井佳久;丸山毅;Makoto Yoshida
通讯作者:
Makoto Yoshida