Visualization of dioxygen bound to copper during enzyme catalysis.
Visualization of dioxygen bound to copper during enzyme catalysis.
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酶催化过程中双氧与铜结合的可视化。
DOI：
10.1126/science.286.5445.1724
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发表时间：
1999
期刊：
影响因子：
56.9
通讯作者：
S. Phillips
中科院分区：
文献类型：
--
作者：
C. Wilmot;J. Hajdu;M. McPherson;P. Knowles;S. Phillips
本文测定了大肠杆菌含铜醌蛋白胺氧化酶氧化半反应中三个相关物种的X射线晶体结构。在暴露于底物后，将晶体在厌氧或需氧条件下冷冻捕获，并将结构确定为2.1和2.4埃之间的分辨率。用单晶分光光度法研究了醌辅因子的氧化态。这些结构揭示了结合双氧的位点和参与氧还原的质子转移途径。醌辅因子通过涉及还原半反应中的催化碱Asp383的水解从亚氨基醌中间体再生。产物醛抑制水解，使得产物的释放成为晶体中反应的速率决定步骤。
X-ray crystal structures of three species related to the oxidative half of the reaction of the copper-containing quinoprotein amine oxidase from Escherichia coli have been determined. Crystals were freeze-trapped either anaerobically or aerobically after exposure to substrate, and structures were determined to resolutions between 2.1 and 2.4 angstroms. The oxidation state of the quinone cofactor was investigated by single-crystal spectrophotometry. The structures reveal the site of bound dioxygen and the proton transfer pathways involved in oxygen reduction. The quinone cofactor is regenerated from the iminoquinone intermediate by hydrolysis involving Asp383, the catalytic base in the reductive half-reaction. Product aldehyde inhibits the hydrolysis, making release of product the rate-determining step of the reaction in the crystal.
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影响因子：
5.7
作者：
Kumar, V;Dooley, DM;Zubak, VM
通讯作者：
Zubak, VM
影响因子：
2.9
作者：
JANES, SM;PALCIC, MM;KLINMAN, JP
通讯作者：
KLINMAN, JP
探究质子耦合电子转移至双氧的机制：牛血清胺氧化酶的氧化半反应。
DOI：
10.1021/bi981103l
发表时间：
1998
期刊：
Biochemistry.
影响因子：
--
作者：
Su,Q;Klinman,JP
通讯作者：
Klinman,JP
影响因子：
2.9
作者：
HARTMANN, C;KLINMAN, JP
通讯作者：
KLINMAN, JP