Characterization of the NuoM (ND4) Subunit in Escherichia coli NDH-1: CONSERVED CHARGED RESIDUES ESSENTIAL FOR ENERGY-COUPLED ACTIVITIES.

Characterization of the NuoM (ND4) Subunit in Escherichia coli NDH-1: CONSERVED CHARGED RESIDUES ESSENTIAL FOR ENERGY-COUPLED ACTIVITIES. Research Abstract Details 

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Characterization of the NuoM (ND4) Subunit in Escherichia coli NDH-1: CONSERVED CHARGED RESIDUES ESSENTIAL FOR ENERGY-COUPLED ACTIVITIES. Abstract Text:

Jesus Torres-Bacete,Eiko Nakamaru-Ogiso,Akemi Matsuno-Yagi,Takao Yagi,Jesus Torres-Bacete,Eiko Nakamaru-Ogiso,Akemi Matsuno-Yagi,Takao Yagi,Jesus Torres-Bacete,Eiko Nakamaru-Ogiso,Akemi Matsuno-Yagi,Takao Yagi,

The proton-translocating NADH-quinone (Q) oxidoreductase (NDH-1) from Escherichia coli is composed of two segments: a peripheral arm and a membrane arm. The membrane arm contains 7 hydrophobic subunits. Of these subunits, NuoM, a homolog of the mitochondrial ND4 subunit, is proposed to be involved in proton translocation and Q-binding. Therefore, we conducted site-directed mutation of 15 amino acid residues of NuoM and investigated their properties. In all mutants, the assembly of the whole enzyme seemed intact. Mutation of highly conserved Glu(144) and Lys(234) leads to almost total elimination of energy-transducing NDH-1 activities as well as increased production of superoxide radicals. Their NADH dehydrogenase activities were almost normal. Because these two residues are predicted to be located in the transmembrane segments of NuoM, the results strongly suggest that they participate in proton translocation. Although it is hypothesized that His interacts with a Q head group, mutations at four His moderately inhibited NDH-1 activities and had almost no effect on the K(m) values for Q or IC(50) values of capsaicin-40, a competitive inhibitor for the Q binding site. The data suggest that these His are not involved in the catalytic Q-binding. Functional roles of NuoM and advantages of NDH-1 research as a model for mitochondrial complex I study have been discussed.

Characterization of the NuoM (ND4) Subunit in Escherichia coli NDH-1: CONSERVED CHARGED RESIDUES ESSENTIAL FOR ENERGY-COUPLED ACTIVITIES. Publishing Authors By Initials

J Torres-Bacete,E Nakamaru-Ogiso,A Matsuno-Yagi,T Yagi,J Torres-Bacete,E Nakamaru-Ogiso,A Matsuno-Yagi,T Yagi,J Torres-Bacete,E Nakamaru-Ogiso,A Matsuno-Yagi,T Yagi,

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Characterization of the NuoM (ND4) Subunit in Escherichia coli NDH-1: CONSERVED CHARGED RESIDUES ESSENTIAL FOR ENERGY-COUPLED ACTIVITIES. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: The Journal of biological chemistry

VOLUME: 282

Page Numbers: 36914-22

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 31

MONTH: 10

YEAR: 2007

Characterization of the NuoM (ND4) Subunit in Escherichia coli NDH-1: CONSERVED CHARGED RESIDUES ESSENTIAL FOR ENERGY-COUPLED ACTIVITIES. Information

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LANGUAGE: eng

NlmUniqueID: 2985121

Characterization of the NuoM (ND4) Subunit in Escherichia coli NDH-1: CONSERVED CHARGED RESIDUES ESSENTIAL FOR ENERGY-COUPLED ACTIVITIES. Keywords Mesh Terms:

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Grant and Affiliation Information for Characterization of the NuoM (ND4) Subunit in Escherichia coli NDH-1: CONSERVED CHARGED RESIDUES ESSENTIAL FOR ENERGY-COUPLED ACTIVITIES.

AFFILIATION: Division of Biochemistry, Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, California 92037.

Country: United States

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MEDLINETA: J Biol Chem

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