MoaA of Arthrobacter nicotinovorans pAO1 involved in Mo-Pterin cofactor synthesis is an Fe-S protein

被引：33

作者：

Menendez, C

Siebert, D

Brandsch, R

机构：

[1] INST BIOCHEM & MOL BIOL,D-79104 FREIBURG,GERMANY

[2] INST PHYS CHEM 2,D-79104 FREIBURG,GERMANY

来源：

FEBS LETTERS | 1996年 / 391卷 / 1-2期

关键词：

MoaA; molybdopterin cofactor; Arthrobacter nicotinovorans; Fe-S cluster; Cys mutagenesis;

D O I：

10.1016/0014-5793(96)00712-0

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：

MoaA, involved in an early step in the biosynthesis of the molybdopterin cofactor (MoCo), has not yet been characterized biochemically and the reaction it catalyzes is unknown, We overexpressed MoaA from pAO1 of Arthrobacter nicotinovorans in Escherichia coli as a N-terminal fusion with either glutathione-S-transferase or a 6-histidine tag, The pAO1 encoded MoaA as well as the fusion proteins functionally complement E. coli moaA mutants, Here we show that purified MoaA contains approximately 4 mu M Fe and approximately 3 mu M acid-labile S/mu M protein, EPR spectroscopy revealed a predominant signal at g(av) = 2.01, indicative of a [3Fe-xS] cluster.

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页码：101 / 103

页数：3

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