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Literature summary extracted from

  • Bento, I.; Matias, P.M.; Baptista, A.M.; da Costa, P.N.; van Dongen, W.M.; Saraiva, L.M.; Schneider, T.R.; Soares, C.M.; Carrondo, M.A.
    Molecular basis for redox-Bohr and cooperative effects in cytochrome c3 from Desulfovibrio desulfuricans ATCC 27774: crystallographic and modeling studies of oxidized and reduced high-resolution structures at pH 7.6 (2004), Proteins, 54, 135-152.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.12.2.1 X-ray diffraction structure determination and analysis of purified reduced cytochrome C3, which is associated with the enzyme, at 0.1 M Tris-HCl, pH 7.6, and 60% PEG 400, at 1.35-1.4 A resolution, comparison to the structure of oxidized cytochrome c3 at pH 4.0, overview, modeling Desulfovibrio desulfuricans

Organism

EC Number Organism UniProt Comment Textmining
1.12.2.1 Desulfovibrio desulfuricans
-
 ATCC 27774
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.12.2.1 H2 + ferricytochrome c3
-
 Desulfovibrio desulfuricans H+ + ferrocytochrome c3
-
 ?
1.12.2.1 additional information the enzyme is associated to cytochrome c3, a tetraheme 13 kDa metalloprotein, analysis of electron binding, cooperativity effects, the Redox-Bohr effect, and thermodynamics of cytochrome c3 Desulfovibrio desulfuricans ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.12.2.1 More the enzyme is associated to cytochrome c3, a tetraheme 13 kDa metalloprotein, structure analysis, modeling study Desulfovibrio desulfuricans

Cofactor

EC Number Cofactor Comment Organism Structure
1.12.2.1 cytochrome c3 the enzyme is associated to cytochrome c3, a tetraheme 13 kDa metalloprotein, analysis of electron binding, cooperativity effects, the Redox-Bohr effect, and thermodynamics of cytochrome c3 Desulfovibrio desulfuricans