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<< < Results 51 - 60 of 61 > >>
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EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Show all pathways known for 7.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 7.1.1.3715399 Substitutions of charged amino acid residues conserved in subunit I perturb the redox metal centers of the Escherichia coli bo-type ubiquinol oxidase J. Biochem. 122 422-429 1997 Escherichia coli ST4676 9378723
Show all pathways known for 7.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 7.1.1.3714141 Substitutions of conserved aromatic amino acid residues in subunit I perturb the metal centers of the Escherichia coli bo-type ubiquinol oxidase Biochemistry 37 1632-1639 1998 Escherichia coli 9484234
Show all pathways known for 7.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 7.1.1.3714141 Substitutions of conserved aromatic amino acid residues in subunit I perturb the metal centers of the Escherichia coli bo-type ubiquinol oxidase Biochemistry 37 1632-1639 1998 Escherichia coli GO103/pMFO2 9484234
Show all pathways known for 7.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 7.1.1.3714308 The quinone-binding sites of the cytochrome bo3 ubiquinol oxidase from Escherichia coli Biochim. Biophys. Acta 1797 1924-1932 2010 Escherichia coli 20416270
Show all pathways known for 7.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 7.1.1.3716311 The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site Nat. Struct. Biol. 7 910-917 2000 Escherichia coli 11017202
Show all pathways known for 7.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 7.1.1.3716735 Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site Proc. Natl. Acad. Sci. USA 102 3657-3662 2005 Escherichia coli 15728392
Show all pathways known for 7.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 7.1.1.3716735 Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site Proc. Natl. Acad. Sci. USA 102 3657-3662 2005 Escherichia coli GO105 15728392
Show all pathways known for 7.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 7.1.1.3715458 Vitreoscilla hemoglobin binds to subunit I of cytochrome bo ubiquinol oxidases J. Biol. Chem. 277 33334-33337 2002 Escherichia coli 12080058
Show all pathways known for 7.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 7.1.1.3715458 Vitreoscilla hemoglobin binds to subunit I of cytochrome bo ubiquinol oxidases J. Biol. Chem. 277 33334-33337 2002 Pseudomonas aeruginosa 12080058
Show all pathways known for 7.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 7.1.1.3715458 Vitreoscilla hemoglobin binds to subunit I of cytochrome bo ubiquinol oxidases J. Biol. Chem. 277 33334-33337 2002 Vitreoscilla sp. 12080058
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