| Autor: |
Menéndez, Cástor, Siebert, Dieter, Brandsch, Roderich |
| Zdroj: |
FEBS Letters; August 1996, Vol. 391 Issue: 1-2 p101-103, 3p |
| Abstrakt: |
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 nicotinovoransin Escherichia colias 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 moaAmutants. 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 gav= 2.01, indicative of a [3Fe‐xS] cluster. |
| Databáze: |
Supplemental Index |
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