Mutations at Asp112 adjacent to the trinuclear Cu center in CueO as the proton donor in the four‐electron reduction of dioxygen

Mutations at Asp112 adjacent to the trinuclear Cu center in CueO as the proton donor in the four‐electron reduction of dioxygen
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DOI:
10.1016/j.febslet.2006.06.049
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发表时间:
2006-07
期刊:
影响因子:
3.5
通讯作者:
Yusaku Ueki;Megumi Inoue;S. Kurose;K. Kataoka;T. Sakurai
Yusaku Ueki;Megumi Inoue;S. Kurose;K. Kataoka;T. Sakurai
中科院分区:
生物学3区
文献类型:
--
作者:
Yusaku Ueki;Megumi Inoue;S. Kurose;K. Kataoka;T. Sakurai

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Asp112位于多铜氧化酶的三核铜中心附近,CueO突变为谷氨酸、丙氨酸和天冬氨酸。Asp112上的突变不仅影响源自三核铜中心的光谱和磁性,而且还影响酶的活性。未配位的Asp112通过促进H+向反应中间产物的供应,促进氧在三核铜中心的结合,加速氧向水分子的转化。
Asp112 adjacent to the trinuclear Cu center of a multicopper oxidase, CueO was mutated for Glu, Ala and Asn. Mutations on Asp112 affected not only spectroscopic and magnetic properties derived from the trinuclear Cu center but also enzyme activities. The uncoordinated Asp112 was found to play multiple roles to promote the binding of dioxygen at the trinuclear Cu center and to accelerate the conversion of dioxygen to water molecules by facilitating the supply of H+to the reaction intermediates.