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Article

The interaction of 5'-adenylylsulfate reductase from Pseudomonas aeruginosa with its substrates.

Biochimica et biophysica acta - 20 Dec 2005

Kim Sung-Kun, Rahman Afroza, Mason Jeremy T, Hirasawa Masakazu, Conover Richard C, Johnson Michael K, Miginiac-Maslow Myroslawa, Keryer Eliane, Knaff David B, Leustek Thomas

Abstract excerpt

APS reductase from Pseudomonas aeruginosa has been shown to form a disulfide-linked adduct with mono-cysteine variants of Escherichia coli thioredoxin and Chlamydomonas reinhardtii thioredoxin h1. These adducts presumably represent trapped versions of the intermediates formed during the catalytic cycle of this thioredoxin-dependent enzyme. The oxidation-reduction midpoint potential of the disulfide bond in the P....

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 16289027
DOI: 10.1016/j.bbabio.2005.09.004

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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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