The C-terminally truncated NuoL subunit (ND5 homologue) of the Na+-dependent complex I from Escherichia coli transports Na+.
about
A 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 subunitsCharacterization of a multigene-encoded sodium/hydrogen antiporter (sha) from Pseudomonas aeruginosa: its involvement in pathogenesisSpecific modification of a Na+ binding site in NADH:quinone oxidoreductase from Klebsiella pneumoniae with dicyclohexylcarbodiimideSingle gene deletions of mrpA to mrpG and mrpE point mutations affect activity of the Mrp Na+/H+ antiporter of alkaliphilic Bacillus and formation of hetero-oligomeric Mrp complexesFeatures of subunit NuoM (ND4) in Escherichia coli NDH-1: TOPOLOGY AND IMPLICATION OF CONSERVED GLU144 FOR COUPLING SITE 1.The role of proton and sodium ions in energy transduction by respiratory complex I.Cation transport by the respiratory NADH:quinone oxidoreductase (complex I): facts and hypotheses.NADH oxidation by the Na+-translocating NADH:quinone oxidoreductase from Vibrio cholerae: functional role of the NqrF subunit.The membrane subunit NuoL(ND5) is involved in the indirect proton pumping mechanism of Escherichia coli complex IThe Staphylococcus aureus NuoL-like protein MpsA contributes to the generation of membrane potential.Roles of subunit NuoL in the proton pumping coupling mechanism of NADH:ubiquinone oxidoreductase (complex I) from Escherichia coliThe deactive form of respiratory complex I from mammalian mitochondria is a Na+/H+ antiporter.The Escherichia coli NADH:ubiquinone oxidoreductase (complex I) is a primary proton pump but may be capable of secondary sodium antiport.Functional roles of four conserved charged residues in the membrane domain subunit NuoA of the proton-translocating NADH-quinone oxidoreductase from Escherichia coli.Characterization of the NuoM (ND4) subunit in Escherichia coli NDH-1: conserved charged residues essential for energy-coupled activities.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.
P2860
Q28488918-2397BFCB-A30C-42B1-865D-F8D6B3EC9C3EQ28492735-C7F8C868-E776-464D-876F-AC07F154D095Q34564971-494A020C-55B7-49E3-8BFA-A9F018B7A725Q36747253-E11B737C-98C6-4326-8D23-BE0F059875AEQ37446025-C6ACFE19-107A-4DD1-A759-F9CFC610754BQ38009270-9D4032BB-1279-4CC3-9254-EF17C8335BF2Q38141074-7BF912DD-59F0-4833-9B87-1D0B6FBAACC1Q38343821-9114AF56-0390-485E-BFE4-BAD02BAEA868Q41175962-B1DA079C-189B-4515-A52B-AB97456D0F7EQ41634510-E74FF824-EBD5-4E0E-BFEF-19660914C2AFQ41646100-6119BBB7-29A8-479A-8AE7-D1023EC165C5Q42021655-D0EC8686-9333-4FDB-8D4B-DD6570A9929CQ44768436-5E861135-E6DD-4B97-87B3-832686CAE07FQ44919453-915D59D6-A0F7-46BC-B861-6536DE60CCA4Q46097074-C17113D0-2002-4909-BA36-106628A69A35Q47317338-52012112-F687-40A5-8165-2C8589570877Q51679864-DFEF96E0-94F5-49D2-989B-314DA77A420F
P2860
The C-terminally truncated NuoL subunit (ND5 homologue) of the Na+-dependent complex I from Escherichia coli transports Na+.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh-hant
name
The C-terminally truncated Nuo ...... cherichia coli transports Na+.
@en
The C-terminally truncated NuoL subunit
@nl
type
label
The C-terminally truncated Nuo ...... cherichia coli transports Na+.
@en
The C-terminally truncated NuoL subunit
@nl
prefLabel
The C-terminally truncated Nuo ...... cherichia coli transports Na+.
@en
The C-terminally truncated NuoL subunit
@nl
P2860
P356
P1476
The C-terminally truncated Nuo ...... cherichia coli transports Na+.
@en
P2093
Julia Steuber
P2860
P304
26817-26822
P356
10.1074/JBC.M301682200
P407
P577
2003-05-10T00:00:00Z