Characterization of the membrane domain subunit NuoJ (ND6) of the NADH-quinone oxidoreductase from Escherichia coli by chromosomal DNA manipulation.
about
Bacteria, yeast, worms, and flies: exploiting simple model organisms to investigate human mitochondrial diseasesMutagenesis of the L, M, and N subunits of Complex I from Escherichia coli indicates a common role in function.Comparative genomics and transcriptomics of trait-gene associationMitochondrial genome analysis of primary open angle glaucoma patientsInsights into the composition and assembly of the membrane arm of plant complex I through analysis of subcomplexes in Arabidopsis mutant lines.Structural contribution of C-terminal segments of NuoL (ND5) and NuoM (ND4) subunits of complex I from Escherichia coli.Apoptosis-inducing Factor (AIF) and Its Family Member Protein, AMID, Are Rotenone-sensitive NADH:Ubiquinone Oxidoreductases (NDH-2).Adaptation of the Mitochondrial Genome in Cephalopods: Enhancing Proton Translocation Channels and the Subunit Interactions.Stoichiometry of proton translocation by respiratory complex I and its mechanistic implications.Electron transfer in subunit NuoI (TYKY) of Escherichia coli NADH:quinone oxidoreductase (NDH-1).Roles of subunit NuoK (ND4L) in the energy-transducing mechanism of Escherichia coli NDH-1 (NADH:quinone oxidoreductase).Semiquinone and cluster N6 signals in His-tagged proton-translocating NADH:ubiquinone oxidoreductase (complex I) from Escherichia coliEnergy transducing roles of antiporter-like subunits in Escherichia coli NDH-1 with main focus on subunit NuoN (ND2)Features of subunit NuoM (ND4) in Escherichia coli NDH-1: TOPOLOGY AND IMPLICATION OF CONSERVED GLU144 FOR COUPLING SITE 1.Essential regions in the membrane domain of bacterial complex I (NDH-1): the machinery for proton translocation.The membrane subunit NuoL(ND5) is involved in the indirect proton pumping mechanism of Escherichia coli complex IMutations in mitochondrial complex III uniquely affect complex I in Caenorhabditis elegans.Pivotal roles of three conserved carboxyl residues of the NuoC (30k) segment in the structural integrity of proton-translocating NADH-quinone oxidoreductase from Escherichia coli.Conserved amino acid residues of the NuoD segment important for structure and function of Escherichia coli NDH-1 (complex I).A new hypothesis on the simultaneous direct and indirect proton pump mechanisms in NADH-quinone oxidoreductase (complex I).Critical roles of subunit NuoH (ND1) in the assembly of peripheral subunits with the membrane domain of Escherichia coli NDH-1Semiquinone intermediates are involved in the energy coupling mechanism of E. coli complex I.Loss of Complex I activity in the Escherichia coli enzyme results from truncating the C-terminus of subunit K, but not from cross-linking it to subunits N or L.Characterization of the NuoM (ND4) subunit in Escherichia coli NDH-1: conserved charged residues essential for energy-coupled activities.
P2860
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P2860
Characterization of the membrane domain subunit NuoJ (ND6) of the NADH-quinone oxidoreductase from Escherichia coli by chromosomal DNA manipulation.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
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2005年學術文章
@zh-hant
name
Characterization of the membra ...... chromosomal DNA manipulation.
@en
Characterization of the membrane domain subunit NuoJ
@nl
type
label
Characterization of the membra ...... chromosomal DNA manipulation.
@en
Characterization of the membrane domain subunit NuoJ
@nl
prefLabel
Characterization of the membra ...... chromosomal DNA manipulation.
@en
Characterization of the membrane domain subunit NuoJ
@nl
P2093
P356
P1433
P1476
Characterization of the membra ...... chromosomal DNA manipulation.
@en
P2093
Akemi Matsuno-Yagi
Eiko Nakamaru-Ogiso
Hideto Miyoshi
Mou-Chieh Kao
Salvatore Di Bernardo
Takao Yagi
P304
P356
10.1021/BI0476477
P407
P577
2005-03-01T00:00:00Z