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Article

Characterization of glycerol trinitrate reductase (NerA) and the catalytic role of active-site residues.

Journal of bacteriology - 1 Mar 2004

Marshall Samantha J, Krause Doreen, Blencowe Dayle K, White Graham F

Abstract excerpt

Glycerol trinitrate reductase (NerA) from Agrobacterium radiobacter, a member of the old yellow enzyme (OYE) family of oxidoreductases, was expressed in and purified from Escherichia coli. Denaturation of pure enzyme liberated flavin mononucleotide (FMN), and spectra of NerA during reduction and reoxidation confirmed its catalytic involvement. Binding of FMN to apoenzyme to form the holoenzyme occurred with a...

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Identifiers

PMID: 14996811
DOI: 10.1128/JB.186.6.1802-1810.2004
PMCID: PMC355970

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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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