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首页> 外文期刊>The biochemical journal >Properties of cupric ions in benzylamine oxidase from pig plasma as studied by magnetic-resonance and kinetic methods
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Properties of cupric ions in benzylamine oxidase from pig plasma as studied by magnetic-resonance and kinetic methods

机译：磁性共振和动力学方法研究苄胺氧化酶亚苄胺氧化酶的性质

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pBenzylamine oxidase from pig plasma has been studied by a variety of chemical and physical techniques. 1. Analytical ultracentrifugation, gel electrophoresis and isoelectric-focusing studies suggest that the enzyme is composed of two subunits with closely similar primary structures. 2. E.s.r. and n.m.r. measurements show that the enzyme contains two well-separated (greater than 0.6 nm) Cu2+ ions at chemically distinct sites. Each Cu2+ ion is coordinated by two water molecules, one ‘axial’ and the other ‘equatorial’. Both water molecules undergo fast exchange (10(5)–10(8) s-1) with solvent and are deprotonated in the pH r!ange 8–9, but only the equatorial water molecule is displaced by the inhibitors N3- and CN-. 3. Kinetic and e.s.r. measurements show that azide and cyanide compete against O2 binding and also make the two Cu2+ sites identical. It is concluded that Cu2+ must participate in the re-oxidation of reduced enzyme by molecular O2./p
机译：>来自猪等离子体的苄胺氧化酶通过各种化学和物理技术研究。 1.分析超速离心，凝胶电泳和等电对焦研究表明，酶由两个亚基组成，具有密切相似的主要结构。 2. E.S.R.和n.m.r.测量表明，在化学不同的位点，酶含有两个分离的分离良好（大于0.6nm）Cu 2 +离子。每个Cu2 +离子由两个水分子，一个'轴向'和另一个“赤道”协调。两种水分子都经过快速交换（10（5）-10（8）S-1）溶剂，并在pH r！ange 8-9中取向，但只有赤道水分子被抑制剂N3和CN移位 - 。 3.动力学和E.S.R.测量表明，叠氮化物和氰化物竞争O2结合，并使两个Cu2 +位点相同。得出结论，Cu2 +必须参与通过分子O 2的减少酶的再氧化。

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