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<< < Results 11 - 20 of 31 > >>
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EC Number Inhibitors Commentary Structure
Display the word mapDisplay the reaction diagram Show all sequences 1.14.18.3cyanide less than 2% residual activity at 2 mM Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 1.14.18.3cyanide cyanide treatment of the enzyme removes about 98% of the copper and about 49% of the iron and abolishes all activity Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 1.14.18.3cysteine pMMO Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 1.14.18.3duroquinol increasing duroquinol concentration above 70 mM causes almost total inhibition of enzyme activity Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 1.14.18.3duroquinone noncompetitive inhibitor Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 1.14.18.3EDTA 18.1% residual activity at 1.5 mM Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 1.14.18.3Fe2+ slightly, membrane-bound enzyme form Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 1.14.18.3Fe2+ 0.75 to two iron ions per protomer. Di-iron may be the pMMO active site Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 1.14.18.3H2O2 reversible inhibition of pMMO with H2O2 upon treatment of pMMO with H2O2 followed by the addition of catalase. H2O2 re-oxidizes the type 2 copper in pMMO reduced with duroquinol Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 1.14.18.3KCN pMMO Go to the Ligand Summary Page
<< < Results 11 - 20 of 31 > >>
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