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Article

Role of hydrogen bonding in the active site of human manganese superoxide dismutase.

Biochemistry - 8 Jun 2004

Greenleaf William B, Perry J Jefferson P, Hearn Amy S, Cabelli Diane E, Lepock James R, Stroupe M Elizabeth, Tainer John A, Nick Harry S, Silverman David N

Abstract excerpt

The side chain of Gln143, a conserved residue in manganese superoxide dismutase (MnSOD), forms a hydrogen bond with the manganese-bound solvent and is critical in maintaining catalytic activity. The side chains of Tyr34 and Trp123 form hydrogen bonds with the carboxamide of Gln143. We have replaced Tyr34 and Trp123 with Phe in single and double mutants of human MnSOD and measured their catalytic activity by...

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Identifiers

PMID: 15170341
DOI: 10.1021/bi049888k

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

Source receipt: pubmed, retrieved 7 Sept 2026.

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