Redox potential of the haem c group in the quinocytochrome, lupanine hydroxylase, an enzyme located in the periplasm of a Pseudomonas sp.

被引：4

作者：

Hopper, DJ ^{[1
]}

Rogozinski, J

机构：

[1] Univ Wales, Inst Biol Sci, Aberystwyth SY23 3DD, Ceredigion, Wales

[2] Acad Agr, Dept Biochem, Inst Plant Biol, PL-02528 Warsaw, Poland

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1998年 / 1383卷 / 01期

关键词：

cytochrome c; quinocytochrome; PQQ; redox potential; lupanine hydroxylase; reconstitution;

D O I：

10.1016/S0167-4838(97)00204-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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. (C) 1998 Elsevier Science B.V.

引用

页码：160 / 164

页数：5

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