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首页> 外文期刊>Biochimica et Biophysica Acta. Protein Structure and Molecular Enzymology >Redox potential of the heam c group in the quinocytochrome, lupanine hydroxylase, an enzyme located in the periplasm of a Pseudomonas sp.
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Redox potential of the heam c group in the quinocytochrome, lupanine hydroxylase, an enzyme located in the periplasm of a Pseudomonas sp.

机译:喹诺酮细胞​​色素,Lupanine羟化酶(位于假单胞菌属种的周质中的一种酶)中的heam c组的氧化还原电位。

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摘要

The quinocytochrome c, lupanine hydroxylase, was shown to be located in the periplasm of a Pseudomonas sp. The midpoint redox potential of the haem in the purified enzyme was measured by potentiometric titration and shown to be + 193 mV. PQQ was removed from the enzyme by isoelectric focusing to give inactive apoenzyme. This resulted in a shift in the midpoint redox potential of the haem to + 98 mV. Full activity was recovered by the addition of PQQ to apoenzyme that also restored the original potential.
机译:奎诺细胞色素c,Lupanine羟化酶,显示位于假单胞菌属的周质中。通过电位滴定法测量纯化酶中血红素的中点氧化还原电势,显示为+ 193 mV。通过等电聚焦从酶中除去PQQ,得到失活的脱辅酶。这导致血红素的中点氧化还原电势转变为+ 98 mV。通过向脱辅酶中添加PQQ恢复了全部活性,这也恢复了原始潜力。

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