The catalytic mechanism of dye‐decolorizing peroxidase DyP may require the swinging movement of an aspartic acid residue
The catalytic mechanism of dye‐decolorizing peroxidase DyP may require the swinging movement of an aspartic acid residue
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染料脱色过氧化物酶 DyP 的催化机制可能需要天冬氨酸残基的摆动运动
DOI：
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发表时间：
2011
期刊：
影响因子：
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通讯作者：
Y. Sugano
中科院分区：
文献类型：
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作者：
Toru Yoshida;H. Tsuge;H. Konno;T. Hisabori;Y. Sugano
染料脱色过氧化物酶（DyP）型过氧化物酶家族是一个独特的血红素过氧化物酶家族。该家族的一级和三级结构明显不同于其它血红素过氧化物酶。然而，这个家族的结构-功能关系的细节仍然知之甚少。我们展示了DyP（EC1.11.1.19）的四种高分辨率结构，这是该家族的代表：天然DyP（1.40 kDa），D171 N突变体DyP（1.42 kDa），天然DyP与氰化物复合（1.45 kDa），以及D171 N突变体DyP与氰化物相关（1.40 kDa）。 这些结构包含形成过氧化氢结合口袋的四个氨基酸，并且它们在该家族中非常保守。此外，这些结构表明Asp 171的OD 2在化合物I形成中接受来自过氧化氢的质子，并且OD 2可以响应于血红素铁的配体摆动到适当的位置。 在这些结果的基础上，我们提出了化合物I形成的摆动机制。 当DyP与过氧化氢反应时，OD 2向最佳位置摆动以接受来自与血红素铁结合的过氧化氢的质子。
The dye‐decolorizing peroxidase (DyP)‐type peroxidase family is a unique heme peroxidase family. The primary and tertiary structures of this family are obviously different from those of other heme peroxidases. However, the details of the structure–function relationships of this family remain poorly understood. We show four high‐resolution structures of DyP (EC1.11.1.19), which is representative of this family: the native DyP (1.40 Å), the D171N mutant DyP (1.42 Å), the native DyP complexed with cyanide (1.45 Å), and the D171N mutant DyP associated with cyanide (1.40 Å). These structures contain four amino acids forming the binding pocket for hydrogen peroxide, and they are remarkably conserved in this family. Moreover, these structures show that OD2 of Asp171 accepts a proton from hydrogen peroxide in compound I formation, and that OD2 can swing to the appropriate position in response to the ligand for heme iron. On the basis of these results, we propose a swing mechanism in compound I formation. When DyP reacts with hydrogen peroxide, OD2 swings towards an optimal position to accept the proton from hydrogen peroxide bound to the heme iron.
DOI：
10.1016/s0021-9258(19)70630-9
发表时间：
1980-09
期刊：
The Journal of biological chemistry
影响因子：
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作者：
T. Poulos;J. Kraut
通讯作者：
T. Poulos;J. Kraut