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Article

13C-, 15N- and 31P-NMR studies of oxidized and reduced low molecular mass thioredoxin reductase and some mutant proteins.

European journal of biochemistry - 1 Apr 2004

Eisenreich Wolfgang, Kemter Kristina, Bacher Adelbert, Mulrooney Scott B, Williams Charles H, Müller Franz

Abstract excerpt

Thioredoxin reductase (TrxR) from Escherichia coli, the mutant proteins E159Y and C138S, and the mutant protein C138S treated with phenylmercuric acetate were reconstituted with [U-(13)C(17),U-(15)N(4)]FAD and analysed, in their oxidized and reduced states, by (13)C-, (15)N- and (31)P-NMR spectroscopy. The enzymes studied showed very similar (31)P-NMR spectra in the oxidized state, consisting of two peaks at -9.8...

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Identifiers

PMID: 15066170
DOI: 10.1111/j.1432-1033.2004.04043.x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

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