MoaA of Arthrobacter nicotinovorans pAO1 involved in Mo‐Pterin cofactor synthesis is an Fe‐S protein
- 5 August 1996
- journal article
- Published by Wiley in FEBS Letters
- Vol. 391 (1-2) , 101-103
- https://doi.org/10.1016/0014-5793(96)00712-0
Abstract
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 μM Fe and approximately 3 μM acid-labile S/μM protein. EPR spectroscopy revealed a predominant signal at g av = 2.01, indicative of a [3Fe-xS] cluster.Keywords
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