51v Solid-state Magic Angle Spinning Nmr Spectroscopy of Vanadium Chloroperoxidase.
From: Brown Laboratories, Department of Chemistry and Biochemistry, University of Delaware, Newark, Delaware 19716, USA.
Journal of the American Chemical Society
- Publish Date: Apr 2006
- ISSN: 0002-7863
- Volume: 128
- Issue: 15
- Pages: 5190-208
- Medium: Print
- Language: English
- Citation (JAMA): Pooransingh-Margolis Neela, Renirie Rokus, Hasan Zulfiqar, et al. 51v Solid-state Magic Angle Spinning Nmr Spectroscopy of Vanadium Chloroperoxidase.. J. Am. Chem. Soc. Apr 2006;128:5190-208
Abstract
We report 51V solid-state NMR spectroscopy of the 67.5-kDa vanadium chloroperoxidase, at 14.1 T. We demonstrate that, despite the low concentration of vanadium sites in the protein (one per molecule, 1 mumol of vanadium spins in the entire sample), the spinning sideband manifold spanning the central and the satellite transitions is readily detectable. The quadrupolar and chemical shift anisotropy tensors have been determined by numerical simulations of the spinning sideband envelopes and the line shapes of the individual spinning sidebands corresponding to the central transition. The observed quadrupolar coupling constant C(Q) of 10.5 +/- 1.5 MHz and chemical shift anisotropy delta(sigma) of -520 +/- 13 ppm are sensitive reporters of the geometric and electronic structure of the vanadium center. Density functional theory calculations of the NMR spectroscopic observables for an extensive series of active site models indicate that the vanadate cofactor is most likely anionic with one axial hydroxo- group and an equatorial plane consisting of one hydroxo- and two oxo- groups. The work reported in this manuscript is the first example of 51V solid-state NMR spectroscopy applied to probe the vanadium center in a protein directly. This approach yields the detailed coordination environment of the metal unavailable from other experimental measurements and is expected to be generally applicable for studies of diamagnetic vanadium sites in metalloproteins.
Mesh Headings (Keywords): Binding Sites, Chloride Peroxidase, Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Vanadium
Check for Full Text / PubMed Unique Identifier (PMID): 16608356
This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.
Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.
The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.