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Article

ENDOR spectroscopy shows that guanine N1 binds to [4Fe-4S] cluster II of the S-adenosylmethionine-dependent enzyme MoaA: mechanistic implications.

Journal of the American Chemical Society - 8 Jul 2009

Lees Nicholas S, Hänzelmann Petra, Hernandez Heather L, Subramanian Sowmya, Schindelin Hermann, Johnson Michael K, Hoffman Brian M

Abstract excerpt

The S-adenosylmethionine-dependent enzyme MoaA, in concert with MoaC, catalyzes the first step of molybdenum cofactor biosynthesis, the conversion of guanosine 5'-triphosphate (5'-GTP) into precursor Z. A published X-ray crystal structure of MoaA with the substrate 5'-GTP revealed that the substrate might be bound to the unique iron of one of two 4Fe-4S clusters through either or both the amino and N1 nitrogen...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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PMID: 19566093
DOI: 10.1021/ja903978u
PMCID: PMC2757093

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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