Toward a characterization of the connecting module of complex I
Complex I [NADH-ubiquinone oxidoreductase (complex I, EC 1.6.5.3)] couples electron transfer between NADH and ubiquinone to proton transport across the bacterial cytoplasmic membrane and the mitochondrial inner membrane. This sophisticated enzyme consists of three specialized modules: (1) a hydrophilic NADH-oxidizing module that constitutes the input machinery of the enzyme; (2) a hydrophobic module that anchors the enzyme in the membrane and must take part in proton transport; and (3) a connecting domain that links the two previous modules. Using the complex I of Rhodobacter capsulatus, we developed a genetic study of the structure and function of the connecting module. In the present review, we put together the salient results of these studies, with recent reports of the literature, to try and elucidate the structure of the connecting module and its potential role in the coupling process between electron and proton flux within complex I. From this overview, we conclude that the NUOB-NUOD dimer of the connecting module and a hydrophobic subunit such as NUOH must share a quinone-reduction site. The function of this site in the mechanism of complex I is discussed.
| Medienart: |
Artikel |
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| Erscheinungsjahr: |
2001 |
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| Erschienen: |
2001 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:33 |
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| Enthalten in: |
Journal of bioenergetics and biomembranes - 33(2001), 3 vom: 08. Juni, Seite 159-68 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Dupuis, A [VerfasserIn] |
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| Themen: |
EC 1.6.- |
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| Anmerkungen: |
Date Completed 12.04.2002 Date Revised 10.12.2019 published: Print Citation Status MEDLINE |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM115887857 |
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| 100 | 1 | |a Dupuis, A |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Toward a characterization of the connecting module of complex I |
| 264 | 1 | |c 2001 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a ohne Hilfsmittel zu benutzen |b n |2 rdamedia | ||
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| 500 | |a Date Completed 12.04.2002 | ||
| 500 | |a Date Revised 10.12.2019 | ||
| 500 | |a published: Print | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Complex I [NADH-ubiquinone oxidoreductase (complex I, EC 1.6.5.3)] couples electron transfer between NADH and ubiquinone to proton transport across the bacterial cytoplasmic membrane and the mitochondrial inner membrane. This sophisticated enzyme consists of three specialized modules: (1) a hydrophilic NADH-oxidizing module that constitutes the input machinery of the enzyme; (2) a hydrophobic module that anchors the enzyme in the membrane and must take part in proton transport; and (3) a connecting domain that links the two previous modules. Using the complex I of Rhodobacter capsulatus, we developed a genetic study of the structure and function of the connecting module. In the present review, we put together the salient results of these studies, with recent reports of the literature, to try and elucidate the structure of the connecting module and its potential role in the coupling process between electron and proton flux within complex I. From this overview, we conclude that the NUOB-NUOD dimer of the connecting module and a hydrophobic subunit such as NUOH must share a quinone-reduction site. The function of this site in the mechanism of complex I is discussed | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Review | |
| 650 | 7 | |a Protein Subunits |2 NLM | |
| 650 | 7 | |a Quinones |2 NLM | |
| 650 | 7 | |a NADH, NADPH Oxidoreductases |2 NLM | |
| 650 | 7 | |a EC 1.6.- |2 NLM | |
| 650 | 7 | |a Electron Transport Complex I |2 NLM | |
| 650 | 7 | |a EC 7.1.1.2 |2 NLM | |
| 700 | 1 | |a Prieur, I |e verfasserin |4 aut | |
| 700 | 1 | |a Lunardi, J |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Journal of bioenergetics and biomembranes |d 1976 |g 33(2001), 3 vom: 08. Juni, Seite 159-68 |w (DE-627)NLM000100501 |x 1573-6881 |7 nnns |
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