Multistep binding of transition metals to the H-N-H endonuclease toxin colicin E9.

Journal article

We report the first stopped-flow fluorescence analysis of transition metal binding (Co(2+), Ni(2+), Cu(2+), and Zn(2+)) to the H-N-H endonuclease motif within colicin E9 (the E9 DNase). The H-N-H consensus forms the active site core of a number of endonuclease groups but is also structurally homologous to the so-called treble-clef motif, a ubiquitous zinc-binding motif found in a wide variety of metalloproteins. We find that all the transition metal ions tested bind via multistep mechanisms. ...

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Authors: Keeble, A; Hemmings, A; James, R; Moore, G; Kleanthous, K

• Journal: Biochemistry
• Volume: 41
• Issue: 32
• Pages: 10234-10244
• Publication date: 2002-08-01
• DOI: 10.1021/bi020174o
• EISSN: 1520-4995
• ISSN: 0006-2960
• Language: English
• Keywords: Zinc; Cations, Divalent; Binding Sites; Copper; Cobalt; Kinetics; Mutagenesis, Site-Directed; Metals, Heavy; Zinc Fingers; Bacterial Toxins; Deoxyribonucleases; Nickel; Phenylalanine; Colicins; Spectrometry, Fluorescence; Tryptophan; Protein Conformation