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Article

The role of the invariant glutamate 95 in the catalytic site of Complex I from Escherichia coli.

Biochimica et biophysica acta - 1 Jan 2009

Euro Liliya, Belevich Galina, Bloch Dmitry A, Verkhovsky Michael I, Wikström Mårten, Verkhovskaya Marina

Abstract excerpt

Replacement of glutamate 95 for glutamine in the NADH- and FMN-binding NuoF subunit of E. coli Complex I decreased NADH oxidation activity 2.5-4.8 times depending on the used electron acceptor. The apparent K(m) for NADH was 5.2 and 10.4 microM for the mutant and wild type, respectively. Analysis of the inhibitory effect of NAD(+) on activity showed that the E95Q mutation caused a 2.4-fold decrease of K(i)(NAD+)...

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Source

Identifiers

PMID: 19061856
DOI: 10.1016/j.bbabio.2008.11.002

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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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