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Manganese(II) active site mutants of 3,4-dihydroxyphenylacetate 2,3-dioxygenase from Arthrobacter globiformis strain CM-2.

Biochemistry - 25 Feb 1997

Boldt Y R, Whiting A K, Wagner M L, Sadowsky M J, Que L, Wackett L P

Abstract excerpt

Whereas all other members of the extradiol-cleaving catechol dioxygenase family are iron-dependent, the 3,4-dihydroxyphenylacetate 2,3-dioxygenase (MndD) from Arthrobacter globiformis CM-2 is dependent on manganese for catalytic activity. Recently, the endogenous iron ligands of one family member, the 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC), were identified crystallographically as two histidines and a...

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PMID: 9047314
DOI: 10.1021/bi962362i

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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