Electron paramagnetic resonance studies of MN(II) complexes with myosin subfragment 1 and oxygen 17-labeled ligands.

M. R. Webb, D. E. Ash, Thomas S. Leyh, D. R. Trentham, G. H. Reed

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Abstract

Ligands in the first coordination sphere of Mn(II) in the complex of MnADP with myosin subfragment 1 from rabbit skeletal muscle have been investigated. EPR spectroscopy was used to detect superhyperfine coupling between unpaired electrons of the metal ion and the nuclei of oxygen atoms specifically labeled with oxygen 17. The results show that ADP is a beta-monodentate ligand for Mn(II) and that there are probably two water oxygens directly bound to Mn(II). The inhibitory complex of vanadate with subfragment 1 . MnADP was also investigated. Vanadate-dependent changes in the EPR spectra for enzyme-bound Mn(II) indicate that the coordination sphere of MN(II) changes upon binding of vanadate. ADP remains a beta-monodenate ligand in the complex and experiments with 17O-labeled water indicate that two oxygen atoms originally in water are ligands in the complex. However, the oxygens of vanadate equilibrate with those of water during sample preparation so that one of these ligands may be a vanadate oxygen. Three additional ligands, probably from the protein, are required to complete the sextet of ligands to Mn(II) in both complexes studied.

Original languageEnglish (US)
Pages (from-to)3068-3072
Number of pages5
JournalJournal of Biological Chemistry
Volume257
Issue number6
StatePublished - Mar 25 1982
Externally publishedYes

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Myosin Subfragments
Electron Spin Resonance Spectroscopy
Paramagnetic resonance
Vanadates
Oxygen
Ligands
Water
Adenosine Diphosphate
Atoms
Metal ions
Muscle
Spectrum Analysis
Skeletal Muscle
Metals
Spectroscopy
Electrons
Ions
Rabbits
Enzymes

ASJC Scopus subject areas

  • Biochemistry

Cite this

Electron paramagnetic resonance studies of MN(II) complexes with myosin subfragment 1 and oxygen 17-labeled ligands. / Webb, M. R.; Ash, D. E.; Leyh, Thomas S.; Trentham, D. R.; Reed, G. H.

In: Journal of Biological Chemistry, Vol. 257, No. 6, 25.03.1982, p. 3068-3072.

Research output: Contribution to journalArticle

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AU - Reed, G. H.

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