Literature summary for 7.1.1.2 extracted from

Narayanan, M.; Sakyiama, J.A.; Elguindy, M.M.; Nakamaru-Ogiso, E.
Roles of subunit NuoL in the proton pumping coupling mechanism of NADH ubiquinone oxidoreductase (complex I) from Escherichia coli (2016), J. Biochem., 160, 205-215 .

Search for more literature for 7.1.1.2

Protein Variants

Protein Variants	Comment	Organism
D178N	mutant of subunit NuoL, about 80% of electron transfer activity of wild-type	Escherichia coli
D303A	mutant of subunit NuoL, about 60% of electron transfer activity of wild-type	Escherichia coli
D3400N	mutant of subunit NuoL, about 35% of electron transfer activity of wild-type	Escherichia coli
D400A	mutant of subunit NuoL, about 80% of electron transfer activity of wild-type	Escherichia coli
D400E	mutant of subunit NuoL, about 50% of electron transfer activity of wild-type	Escherichia coli
E144Q	mutant of subunit NuoL, about 10% of electron transfer activity of wild-type	Escherichia coli
H334Q	mutant of subunit NuoL, about 50% of electron transfer activity of wild-type	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
5-(N-ethyl-N-isopropyl)-amiloride	0.015 mM, up to 40% decrease in the proton pumping activity of the wild-type and subunit NuoL mutants D303A, D400A, D400E, no significant change in mutant D178N	Escherichia coli
Zn2+	at 2 mM Zn2+, proton pumping of the wild-type is selectively inhibited without affecting electron transfer, no inhibition in proton pumping of mutants D178N and D400A	Escherichia coli

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	almost no proton pumping activities detected in the absence of Mg2+	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining

General Information

General Information	Comment	Organism
physiological function	subunit NuoL is involved in the high efficiency pumping mechanism in complex I	Escherichia coli

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Release 2023.1 (January 2023)