NMR assignments of cd-HO, a 24 kDa heme oxygenase from Corynebacterium diphtheria

• Published in: Biomolecular NMR assignments Vol. 1; no. 1; pp. 55 - 56
• Main Authors: Hom, Kellie, Furci, Lena M, Deshmukh, Rahul, Wilks, Angela
• Format: Journal Article
• Language: English
• Published: Netherlands Springer Nature B.V 01.07.2007
• Subjects: Apoenzymes - chemistry; Apoenzymes - genetics; Apoenzymes - metabolism; Bacteria; Bacterial proteins; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Binding Sites; Corynebacterium diphtheriae - enzymology; Corynebacterium diphtheriae - genetics; Heme Oxygenase (Decyclizing) - chemistry; Heme Oxygenase (Decyclizing) - genetics; Heme Oxygenase (Decyclizing) - metabolism; Holoenzymes - chemistry; Holoenzymes - genetics; Holoenzymes - metabolism; Molecular Structure; Nuclear Magnetic Resonance, Biomolecular; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Recombinant Proteins - metabolism
• ISSN: 1874-2718; 1874-270X
• DOI: 10.1007/s12104-007-9014-3

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.