Stopped‐flow spectrophotometric and resonance Raman analyses of aldoxime dehydratase involved in carbon–nitrogen triple bond synthesis
Stopped‐flow spectrophotometric and resonance Raman analyses of aldoxime dehydratase involved in carbon–nitrogen triple bond synthesis
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碳氮三键合成中醛肟脱水酶的停流分光光度法和共振拉曼分析
DOI：
10.1016/j.febslet.2005.01.037
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发表时间：
2005
期刊：
影响因子：
3.5
通讯作者：
Michihiko Kobayashi
中科院分区：
文献类型：
--
作者：
Ken;H. Kumita;T. Ohta;K. Konishi;Y. Hashimoto;H. Higashibata;T. Kitagawa;Y. Shiro;Michihiko Kobayashi
在停流分析中，一种新的血红素蛋白--脂肪醛肟脱水酶(OxdA)在421 nm处由一个反应中间体与丁醛肟亚铁反应产生的光谱逐渐转变为亚铁的等色点。在亚铁H320A突变体中加入丁醛肟后的光谱变化表明，它形成了底物配位突变体，其吸收光谱与上述中间体的吸收光谱非常相似。这些观察和共振拉曼研究表明，底物实际上与OxdA中的血红素结合，形成了六配位的低自旋血红素。
On stopped-flow analysis of aliphatic aldoxime dehydratase (OxdA), a novel hemoprotein, a spectrum derived from a reaction intermediate was detected on mixing ferrous OxdA with butyraldoxime; it gradually changed into that of ferrous OxdA with an isosbestic point at 421nm. The spectral change on the addition of butyraldoxime to the ferrous H320A mutant showed the formation of a substrate-coordinated mutant, the absorption spectrum of which closely resembled that of the above intermediate. These observations and the resonance Raman investigation revealed that the substrate actually binds to the heme in OxdA, forming a hexa-coordinate low-spin heme.
DOI：
10.1073/pnas.94.21.11216
发表时间：
1997-10-14
影响因子：
11.1
作者：
Shelver, D;Kerby, RL;Roberts, GP
通讯作者：
Roberts, GP