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Literature summary for 1.3.5.1 extracted from

  • Cheng, V.W.; Ma, E.; Zhao, Z.; Rothery, R.A.; Weiner, J.H.
    The iron-sulfur clusters in Escherichia coli succinate dehydrogenase direct electron flow (2006), J. Biol. Chem., 281, 27662-27668.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
I150E mutation lowers the midpoint potential of the [4Fe-4S] cluster Escherichia coli
I150H mutation lowers the midpoint potential of the [4Fe-4S] cluster Escherichia coli
L220S mutation does not alter the redox behavior of the [4Fe-4S] cluster but instead lowers the midpoint potential of the [3Fe-4S] cluster Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
succinate + ubiquinone Escherichia coli
-
 fumarate + ubiquinol
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
succinate + ubiquinone
-
 Escherichia coli fumarate + ubiquinol
-
 ?

Cofactor

Cofactor Comment Organism Structure
FAD ubiquinone reduction by an electron transfer relay comprising a flavin adenine dinucleotide cofactor, three iron-sulfur clusters, and possibly a heme b556. At the heart of the electron transport chain is a [4Fe-4S] cluster with a low midpoint potential that acts as an energy barrier against electron transfer Escherichia coli
heme b556 ubiquinone reduction by an electron transfer relay comprising a flavin adenine dinucleotide cofactor, three iron-sulfur clusters, and possibly a heme b556. At the heart of the electron transport chain is a [4Fe-4S] cluster with a low midpoint potential that acts as an energy barrier against electron transfer Escherichia coli
iron-sulfur centre ubiquinone reduction by an electron transfer relay comprising a flavin adenine dinucleotide cofactor, three iron-sulfur clusters, and possibly a heme b556. At the heart of the electron transport chain is a [4Fe-4S] cluster with a low midpoint potential that acts as an energy barrier against electron transfer Escherichia coli