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Article

Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis.

The Journal of biological chemistry - 13 Aug 2004

Hänzelmann Petra, Hernández Heather L, Menzel Christian, García-Serres Ricardo, Huynh Boi Hanh, Johnson Michael K, Mendel Ralf R, Schindelin Hermann

Abstract excerpt

The human proteins MOCS1A and MOCS1B catalyze the conversion of a guanosine derivative to precursor Z during molybdenum cofactor biosynthesis. MOCS1A shares homology with S-adenosylmethionine (AdoMet)-dependent radical enzymes, which catalyze the formation of protein and/or substrate radicals by reductive cleavage of AdoMet through a [4Fe-4S] cluster. Sequence analysis of MOCS1A showed two highly conserved...

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PMID: 15180982
DOI: 10.1074/jbc.M313398200

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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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