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PMID:12374822
| Citation |
Heo, J, Wolfe, MT, Staples, CR and Ludden, PW (2002) Converting the NiFeS carbon monoxide dehydrogenase to a hydrogenase and a hydroxylamine reductase. J. Bacteriol. 184:5894-7 |
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| Abstract |
Substitution of one amino acid for another at the active site of an enzyme usually diminishes or eliminates the activity of the enzyme. In some cases, however, the specificity of the enzyme is changed. In this study, we report that the changing of a metal ligand at the active site of the NiFeS-containing carbon monoxide dehydrogenase (CODH) converts the enzyme to a hydrogenase or a hydroxylamine reductase. CODH with alanine substituted for Cys(531) exhibits substantial uptake hydrogenase activity, and this activity is enhanced by treatment with CO. CODH with valine substituted for His(265) exhibits hydroxylamine reductase activity. Both Cys(531) and His(265) are ligands to the active-site cluster of CODH. Further, CODH with Fe substituted for Ni at the active site acquires hydroxylamine reductase activity. |
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| Keywords |
Acetylene; Aldehyde Oxidoreductases/genetics; Aldehyde Oxidoreductases/metabolism; Bacterial Proteins/metabolism; Cyanides; Hydrogenase/genetics; Hydrogenase/metabolism; Iron-Sulfur Proteins/metabolism; Multienzyme Complexes/genetics; Multienzyme Complexes/metabolism; Oxidoreductases/genetics; Oxidoreductases/metabolism; Rhodospirillum rubrum/enzymology; Rhodospirillum rubrum/genetics |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0050418: hydroxylamine reductase activity |
ECO:0000314: |
F |
Substrate dependence of hydroxylamine reduction by various forms of CODH. Hydroxylamine (NH2OH) reductase activities with variable concentrations of NH2OH were monitored as described in Fig 1. |
complete | ||||
See also
References
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