AI Article Synopsis
- * The study provides nearly complete chemical shift assignments for a 215-amino acid heme oxygenase (HO) from Corynebacterium diphtheria in different forms.
- * These assignments will help determine which parts of the heme oxygenase change when binding to compounds, aiding the development of specific inhibitors for these bacterial proteins.
Article Abstract
We are employing a number of selective in vitro and in vivo methods including NMR to screen compounds that bind to heme oxygenases from pathogenic bacteria. We report the nearly complete HN, N, CO, Calpha and Cbeta chemical shift assignments of a 215-amino acid HO from Corynebacterium diphtheria in three forms, apo cd-HO-G135A, apo cd-HO and CO-bound ferrous holo cd-HO; these assignments will enable us to identify residues on cd-HO that are perturbed upon binding to selected compounds, and to help with the development of inhibitors specific to the bacterial proteins.
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| http://dx.doi.org/10.1007/s12104-007-9014-3 | DOI Listing |
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