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Literature summary for 7.1.1.8 extracted from

  • Woronowicz, K.; Sha, D.; Frese, R.N.; Sturgis, J.N.; Nanda, V.; Niederman, R.A.
    The effects of protein crowding in bacterial photosynthetic membranes on the flow of quinone redox species between the photochemical reaction center and the ubiquinol-cytochrome c2 oxidoreductase (2011), Metallomics, 3, 765-774.
    View publication on PubMed
Search for more literature for 7.1.1.8

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane membrane localization and organization of enzyme complex domains, overview Cereibacter sphaeroides 16020
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membrane membrane localization and organization of enzyme complex domains, overview Magnetospirillum molischianum 16020
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additional information architecture of the intracytoplasmic membrane, overview Cereibacter sphaeroides
-
-
additional information architecture of the intracytoplasmic membrane, overview Magnetospirillum molischianum
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ubiquinol + 2 ferricytochrome c Cereibacter sphaeroides
-
 ubiquinone + 2 ferrocytochrome c + 2 H+
-
 ?
ubiquinol + 2 ferricytochrome c Magnetospirillum molischianum
-
 ubiquinone + 2 ferrocytochrome c + 2 H+
-
 ?

Organism

Organism UniProt Comment Textmining
Cereibacter sphaeroides
-
-
-
Magnetospirillum molischianum
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ubiquinol + 2 ferricytochrome c
-
 Cereibacter sphaeroides ubiquinone + 2 ferrocytochrome c + 2 H+
-
 ?
ubiquinol + 2 ferricytochrome c
-
 Magnetospirillum molischianum ubiquinone + 2 ferrocytochrome c + 2 H+
-
 ?

Synonyms

Synonyms Comment Organism
ubiquinol-cytochrome c2 oxidoreductase
-
 Cereibacter sphaeroides
ubiquinol-cytochrome c2 oxidoreductase
-
 Magnetospirillum molischianum

General Information

General Information Comment Organism
additional information mechanisms of quinone redox species flow in the intracytoplasmic membrane bilayer, overview. The enzyme complex from Phaeospirillum molischianum shows a more random organization and slower reaction center turnover compared to the enzyme complex from Rhodobacter sphaeroides Magnetospirillum molischianum
additional information mechanisms of quinone redox species flow in the intracytoplasmic membrane bilayer, overview. The enzyme shows a highly organized arrangement of light harvesting and reaction center complexes and fast reaction center electron transfer turnover. Cytochrome bc1 or ATPase complexes are localized in membrane domains distinct from the flat regions. Modeling of subunit IV into the cytochrome bc1 complex Cereibacter sphaeroides