Kinetics of metal binding by a zinc finger peptide

Jeffrey C. Buchsbaum, Jeremy M. Berg

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

The kinetics of cobalt(II) and zinc(II) binding by a prototypical zinc finger peptide has been examined by stopped-flow spectrometry. Cobalt(II) binding was demonstrated to be second order, first order in each peptide and cobalt(II) concentration. At pH 6.55 in 100 mM HEPES, 100 mM NaCl buffer the second order rate constant was 7.5(± 2.1) x 104 M-1 s-1. The displacement of cobalt(II) by zinc(II) was examined at pH 7.0 as a function of both cobalt(II) and zinc(II) concentration. The data are consistent with a dissociative mechanism with the rate of zinc(II) binding being substantially faster than cobalt(II) binding. The rate constant for cobalt(II) dissociation was 5.3(± 0.5) x 10-2 s-1. The ratio of the rate constants for zinc(II) and cobalt(II) binding was found to be 66 ± 3, indicating that the rate constant for zinc(II) is 2.8(± 0.4) x 107 M-1 s-1 at pH 7.0. This indicates that the rate of zinc(II) dissociation is of 1.6(± 0.6) x 10-4 s-1. The magnitude of the kinetic preference for zinc(II) over cobalt(II) revealed in metal binding rate constants is observed for many other zinc metalloproteins despite the fact that these rate constants vary over eight orders of magnitude. (C) 2000 Elsevier Science S.A.

Original languageEnglish (US)
Pages (from-to)217-219
Number of pages3
JournalInorganica Chimica Acta
Volume297
Issue number1-2
DOIs
StatePublished - 2000
Externally publishedYes

Fingerprint

Zinc Fingers
Cobalt
Peptides
peptides
Zinc
zinc
Metals
cobalt
Kinetics
kinetics
Rate constants
metals
Metalloproteins
HEPES
dissociation
Spectrum Analysis
Spectrometry
Buffers
buffers

Keywords

  • Kinetics
  • Metal binding
  • Stopped-flow spectrometry
  • Zinc finger peptide

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry
  • Physical and Theoretical Chemistry
  • Materials Chemistry

Cite this

Kinetics of metal binding by a zinc finger peptide. / Buchsbaum, Jeffrey C.; Berg, Jeremy M.

In: Inorganica Chimica Acta, Vol. 297, No. 1-2, 2000, p. 217-219.

Research output: Contribution to journalArticle

Buchsbaum, Jeffrey C. ; Berg, Jeremy M. / Kinetics of metal binding by a zinc finger peptide. In: Inorganica Chimica Acta. 2000 ; Vol. 297, No. 1-2. pp. 217-219.
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N2 - The kinetics of cobalt(II) and zinc(II) binding by a prototypical zinc finger peptide has been examined by stopped-flow spectrometry. Cobalt(II) binding was demonstrated to be second order, first order in each peptide and cobalt(II) concentration. At pH 6.55 in 100 mM HEPES, 100 mM NaCl buffer the second order rate constant was 7.5(± 2.1) x 104 M-1 s-1. The displacement of cobalt(II) by zinc(II) was examined at pH 7.0 as a function of both cobalt(II) and zinc(II) concentration. The data are consistent with a dissociative mechanism with the rate of zinc(II) binding being substantially faster than cobalt(II) binding. The rate constant for cobalt(II) dissociation was 5.3(± 0.5) x 10-2 s-1. The ratio of the rate constants for zinc(II) and cobalt(II) binding was found to be 66 ± 3, indicating that the rate constant for zinc(II) is 2.8(± 0.4) x 107 M-1 s-1 at pH 7.0. This indicates that the rate of zinc(II) dissociation is of 1.6(± 0.6) x 10-4 s-1. The magnitude of the kinetic preference for zinc(II) over cobalt(II) revealed in metal binding rate constants is observed for many other zinc metalloproteins despite the fact that these rate constants vary over eight orders of magnitude. (C) 2000 Elsevier Science S.A.

AB - The kinetics of cobalt(II) and zinc(II) binding by a prototypical zinc finger peptide has been examined by stopped-flow spectrometry. Cobalt(II) binding was demonstrated to be second order, first order in each peptide and cobalt(II) concentration. At pH 6.55 in 100 mM HEPES, 100 mM NaCl buffer the second order rate constant was 7.5(± 2.1) x 104 M-1 s-1. The displacement of cobalt(II) by zinc(II) was examined at pH 7.0 as a function of both cobalt(II) and zinc(II) concentration. The data are consistent with a dissociative mechanism with the rate of zinc(II) binding being substantially faster than cobalt(II) binding. The rate constant for cobalt(II) dissociation was 5.3(± 0.5) x 10-2 s-1. The ratio of the rate constants for zinc(II) and cobalt(II) binding was found to be 66 ± 3, indicating that the rate constant for zinc(II) is 2.8(± 0.4) x 107 M-1 s-1 at pH 7.0. This indicates that the rate of zinc(II) dissociation is of 1.6(± 0.6) x 10-4 s-1. The magnitude of the kinetic preference for zinc(II) over cobalt(II) revealed in metal binding rate constants is observed for many other zinc metalloproteins despite the fact that these rate constants vary over eight orders of magnitude. (C) 2000 Elsevier Science S.A.

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