Characterization of the NuoM (ND4) subunit in Escherichia coli NDH-1: conserved charged residues essential for energy-coupled activities.
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The architecture of respiratory complex IA cytochrome c fusion protein domain for convenient detection, quantification, and enhanced production of membrane proteins in Escherichia coli--expression and characterization of cytochrome-tagged Complex I subunitsBacteria, yeast, worms, and flies: exploiting simple model organisms to investigate human mitochondrial diseasesRandomly selected suppressor mutations in genes for NADH : quinone oxidoreductase-1, which rescue motility of a Salmonella ubiquinone-biosynthesis mutant strain.Mutagenesis of the L, M, and N subunits of Complex I from Escherichia coli indicates a common role in function.Identification of a gene essential for protoporphyrinogen IX oxidase activity in the cyanobacterium Synechocystis sp. PCC6803.Single site mutations in the hetero-oligomeric Mrp antiporter from alkaliphilic Bacillus pseudofirmus OF4 that affect Na+/H+ antiport activity, sodium exclusion, individual Mrp protein levels, or Mrp complex formation.Structural contribution of C-terminal segments of NuoL (ND5) and NuoM (ND4) subunits of complex I from Escherichia coli.Stoichiometry of proton translocation by respiratory complex I and its mechanistic implications.Constraining the Lateral Helix of Respiratory Complex I by Cross-linking Does Not Impair Enzyme Activity or Proton Translocation.Electron transfer in subunit NuoI (TYKY) of Escherichia coli NADH:quinone oxidoreductase (NDH-1).Functional Differentiation of Antiporter-Like Polypeptides in Complex I; a Site-Directed Mutagenesis Study of Residues Conserved in MrpA and NuoL but Not in MrpD, NuoM, and NuoN.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)Architecture of complex I and its implications for electron transfer and proton pumping.Features of subunit NuoM (ND4) in Escherichia coli NDH-1: TOPOLOGY AND IMPLICATION OF CONSERVED GLU144 FOR COUPLING SITE 1.The mechanism of coupling between electron transfer and proton translocation in respiratory complex I.Essential regions in the membrane domain of bacterial complex I (NDH-1): the machinery for proton translocation.Symmetry-related proton transfer pathways in respiratory complex I.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).Roles of subunit NuoL in the proton pumping coupling mechanism of NADH:ubiquinone oxidoreductase (complex I) from Escherichia coliA 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.Differences in the phenotypic effects of mutations in homologous MrpA and MrpD subunits of the multi-subunit Mrp-type Na+/H+ antiporter.Probing the proton channels in subunit N of Complex I from Escherichia coli through intra-subunit cross-linking.Mrp Antiporters Have Important Roles in Diverse Bacteria and Archaea.Reconstruction of a human mitochondrial complex I mutation in the unicellular green alga Chlamydomonas.Long-range proton-coupled electron transfer in biological energy conversion: towards mechanistic understanding of respiratory complex I.The Lysine 299 Residue Endows the Multisubunit Mrp1 Antiporter with Dominant Roles in Na+ Resistance and pH Homeostasis in Corynebacterium glutamicum.Prognostic implications and molecular associations of NADH dehydrogenase subunit 4 (ND4) mutations in acute myeloid leukemia.The transmembrane helices of the L, M, and N subunits of Complex I from E. coli can be assigned on the basis of conservation and hydrophobic moment analysis.
P2860
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P2860
Characterization of the NuoM (ND4) subunit in Escherichia coli NDH-1: conserved charged residues essential for energy-coupled activities.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
@zh-hant
name
Characterization of the NuoM ( ...... for energy-coupled activities.
@en
Characterization of the NuoM
@nl
type
label
Characterization of the NuoM ( ...... for energy-coupled activities.
@en
Characterization of the NuoM
@nl
prefLabel
Characterization of the NuoM ( ...... for energy-coupled activities.
@en
Characterization of the NuoM
@nl
P2093
P2860
P356
P1476
Characterization of the NuoM ( ...... for energy-coupled activities.
@en
P2093
Akemi Matsuno-Yagi
Eiko Nakamaru-Ogiso
Jesus Torres-Bacete
Takao Yagi
P2860
P304
36914-36922
P356
10.1074/JBC.M707855200
P407
P577
2007-10-31T00:00:00Z