Phosphorus nuclear-magnetic-resonance studies of a transition-state analogue complex of creatine kinase

Milner-White, E. J. and Rycroft, D. S. (1977) Phosphorus nuclear-magnetic-resonance studies of a transition-state analogue complex of creatine kinase. Biochemical Journal : Molecular Aspects, 167(3), pp. 827-829. (doi: 10.1042/bj1670827) (PMID:603637)

Abstract

³¹P nuclear-magnetic-resonance spectra of MgADP bound to creatine kinase in the presence of creatine NO₃⁻ ions show that there are two non-identical forms of the bound nucleotide. The sites have different affinities for the nucleotide. MgADP at the high-affinity site is in slow exchange (k <125s⁻¹ at 27°C) with free MgADP.

• Item Type: Articles
• Keywords: NMR spectroscopy, phosphorus chemistry.
• Status: Published
• Refereed: Yes
• Glasgow Author(s) Enlighten ID: Rycroft, Dr David and Milner-White, Professor E
• Authors: Milner-White, E. J., and Rycroft, D. S.
• Subjects: Q Science > QD Chemistry; Q Science > QH Natural history > QH345 Biochemistry
• College/School: College of Science and Engineering > School of Chemistry; College of Medical Veterinary and Life Sciences > School of Life Sciences
• Journal Name: Biochemical Journal : Molecular Aspects
• Journal Abbr.: Biochem. J.
• Publisher: Portland Press Ltd.
• ISSN: 0306-3275