Structural contribution of C-terminal segments of NuoL (ND5) and NuoM (ND4) subunits of complex I from Escherichia coli.
about
Review: can diet influence the selective advantage of mitochondrial DNA haplotypes?Randomly selected suppressor mutations in genes for NADH : quinone oxidoreductase-1, which rescue motility of a Salmonella ubiquinone-biosynthesis mutant strain.NdhP is an exclusive subunit of large complex of NADPH dehydrogenase essential to stabilize the complex in Synechocystis sp. strain PCC 6803.A giant molecular proton pump: structure and mechanism of respiratory complex I.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).Roles of subunit NuoK (ND4L) in the energy-transducing mechanism of Escherichia coli NDH-1 (NADH:quinone oxidoreductase).Energy transducing roles of antiporter-like subunits in Escherichia coli NDH-1 with main focus on subunit NuoN (ND2)Functional Role of MrpA in the MrpABCDEFG Na+/H+ Antiporter Complex from the Archaeon Methanosarcina acetivorans.Integrative Approaches for Studying Mitochondrial and Nuclear Genome Co-evolution in Oxidative Phosphorylation.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.On the mechanism of respiratory complex I.Oxygenic photosynthesis-specific subunits of cyanobacterial NADPH dehydrogenases.Symmetry-related proton transfer pathways in respiratory complex I.Phylogenomic analysis and predicted physiological role of the proton-translocating NADH:quinone oxidoreductase (complex I) across bacteria.Conserved amino acid residues of the NuoD segment important for structure and function of Escherichia coli NDH-1 (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.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.Respiratory complex I from Escherichia coli does not transport Na(+) in the absence of its NuoL subunit.Long-range proton-coupled electron transfer in biological energy conversion: towards mechanistic understanding of respiratory complex I.
P2860
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P2860
Structural contribution of C-terminal segments of NuoL (ND5) and NuoM (ND4) subunits of complex I from Escherichia coli.
description
2011 nî lūn-bûn
@nan
2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Structural contribution of C-t ...... mplex I from Escherichia coli.
@ast
Structural contribution of C-t ...... mplex I from Escherichia coli.
@en
type
label
Structural contribution of C-t ...... mplex I from Escherichia coli.
@ast
Structural contribution of C-t ...... mplex I from Escherichia coli.
@en
prefLabel
Structural contribution of C-t ...... mplex I from Escherichia coli.
@ast
Structural contribution of C-t ...... mplex I from Escherichia coli.
@en
P2093
P2860
P356
P1476
Structural contribution of C-t ...... mplex I from Escherichia coli.
@en
P2093
Akemi Matsuno-Yagi
Jesus Torres-Bacete
Prem Kumar Sinha
Takao Yagi
P2860
P304
34007-34014
P356
10.1074/JBC.M111.260968
P407
P577
2011-08-11T00:00:00Z