Involvement of Tyrosines 114 and 139 of Subunit NuoB in the Proton Pathway around Cluster N2 inEscherichia coliNADH:Ubiquinone Oxidoreductase
- Standort
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Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
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Online-Ressource
- Sprache
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Englisch
- Anmerkungen
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The journal of biological chemistry : JBC. - 278, 5 (2003) , 3055-3062, ISSN: 0021-9258
- Ereignis
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Veröffentlichung
- (wo)
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Freiburg
- (wer)
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Universität
- (wann)
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2019
- Beteiligte Personen und Organisationen
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Institute of Biochemistry, Molecular Bioenergetics
- DOI
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10.1074/jbc.m208849200
- URN
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urn:nbn:de:bsz:25-freidok-667041
- Rechteinformation
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
25.03.2025, 13:43 MEZ
Datenpartner
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Beteiligte
- Flemming, Dirk
- Hellwig, Petra
- Friedrich, Thorsten
- Institute of Biochemistry, Molecular Bioenergetics
- Universität
Entstanden
- 2019
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Involvement of tyrosines 114 and 139 of subunit NuoB in the proton pathway around cluster N2 in Escherichia coli NADH:ubiquinone oxidoreductase
Catalytic importance of acidic amino acids on subunit NuoB of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I)
Strukturelle Untersuchung der NADH Oxidation durch NuoEF
Iron-sulfur cluster N2 of the escherichia coliNADH:ubiquinone oxidoreductase (complex I) is located on subunit NuoB
Structural robustness of the NADH binding site in NADH:ubiquinone oxidoreductase (complex I)
Assembly of the Escherichia coli NADH:ubiquinone oxidoreductase (respiratory complex I)
The Escherichia coli NADH:ubiquinone oxidoreductase (complex I) is a primary proton pump but may be capable of secondary sodium antiport
Structure of NuoEF variants for the analysis of NADH binding by respiratory complex I
Der Elektronentransfer der Escherichia coli NADH:Ubichinon Oxidoreduktase sowie die ESR-spektroskopische Charakterisierung weiterer Metalloproteine
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Ortsgerichtete Spinsondenmarkierung der Escherichia coli NADH:Ubichinon Oxidoreduktase zur ESR-spektroskopischen Lokalisierung der Ubichinonbindestelle
Involvement of tyrosines 114 and 139 of subunit NuoB in the proton pathway around cluster N2 in Escherichia coli NADH:ubiquinone oxidoreductase
Catalytic importance of acidic amino acids on subunit NuoB of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I)
Strukturelle Untersuchung der NADH Oxidation durch NuoEF
Iron-sulfur cluster N2 of the escherichia coliNADH:ubiquinone oxidoreductase (complex I) is located on subunit NuoB
Structural robustness of the NADH binding site in NADH:ubiquinone oxidoreductase (complex I)
Assembly of the Escherichia coli NADH:ubiquinone oxidoreductase (respiratory complex I)
The Escherichia coli NADH:ubiquinone oxidoreductase (complex I) is a primary proton pump but may be capable of secondary sodium antiport
Structure of NuoEF variants for the analysis of NADH binding by respiratory complex I
Der Elektronentransfer der Escherichia coli NADH:Ubichinon Oxidoreduktase sowie die ESR-spektroskopische Charakterisierung weiterer Metalloproteine
The Ubiquinone-binding Site in NADH:Ubiquinone Oxidoreductase from Escherichia coli
Structure of the ubiquinol:oxygen cytochrome bd-I oxidoreductase from Escherichia coli
Ortsgerichtete Spinsondenmarkierung der Escherichia coli NADH:Ubichinon Oxidoreduktase zur ESR-spektroskopischen Lokalisierung der Ubichinonbindestelle
Involvement of tyrosines 114 and 139 of subunit NuoB in the proton pathway around cluster N2 in Escherichia coli NADH:ubiquinone oxidoreductase
Catalytic importance of acidic amino acids on subunit NuoB of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I)
Strukturelle Untersuchung der NADH Oxidation durch NuoEF
Iron-sulfur cluster N2 of the escherichia coliNADH:ubiquinone oxidoreductase (complex I) is located on subunit NuoB
Structural robustness of the NADH binding site in NADH:ubiquinone oxidoreductase (complex I)
Assembly of the Escherichia coli NADH:ubiquinone oxidoreductase (respiratory complex I)
The Escherichia coli NADH:ubiquinone oxidoreductase (complex I) is a primary proton pump but may be capable of secondary sodium antiport
Structure of NuoEF variants for the analysis of NADH binding by respiratory complex I
Der Elektronentransfer der Escherichia coli NADH:Ubichinon Oxidoreduktase sowie die ESR-spektroskopische Charakterisierung weiterer Metalloproteine
The Ubiquinone-binding Site in NADH:Ubiquinone Oxidoreductase from Escherichia coli
Structure of the ubiquinol:oxygen cytochrome bd-I oxidoreductase from Escherichia coli