31P-1H correlation and resonance assignments along the DNA backbone: three-dimensional implementation of heteronuclear long-range correlation experiment

Rastogi, Vinit K.

doi:10.1002/(sici)1097-458x(200004)38:4<288::aid-mrc636>3.0.co;2-s

Magn. Reson. Chem.

2000

DOI: 10.1002/(sici)1097-458x(200004)38:4<288::aid-mrc636>3.0.co;2-s

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31P-1H correlation and resonance assignments along the DNA backbone: three-dimensional implementation of heteronuclear long-range correlation experiment

Vinit K. Rastogi

Abstract: A three‐dimensional heteronuclear NMR technique to correlate 31P spins with 1H along the backbone of DNA is described. The approach is based on a 31P–1H heteronuclear long‐range correlation (HELCO) experiment in its refocused form. The utility of this technique is demonstrated by the sequence‐specific resonance assignment of 31P and 1H spins along the backbone of a mismatched base‐paired dodecanucleotide, d‐GGTACIAGTACC. Copyright © 2000 John Wiley & Sons, Ltd.

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Probing phosphorylation by non-mammalian isoprenoid biosynthetic enzymes using 1H–31P–31P correlation NMR spectroscopy

et al. 2009

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The biogenesis of isopentenyl pyrophosphate (IPP) and dimethylallyl pyrophosphate (DMAPP) is accomplished by the methylerythritol phosphate (MEP) pathway in plants, bacteria and parasites, making it a potential target for the development of anti-infective agents and herbicides. The biosynthetic enzymes comprising this pathway catalyze intriguing chemical transformations on diphosphate scaffolds, offering an opportunity to generate novel analogs in this synthetically challenging compound class. Such a biosynthetic approach to generating new diphosphate analogs may involve transformation through discrete diphosphate species, presenting unique challenges in structure determination and characterization of unnatural enzyme-generated diphosphate products produced in tandem. We have developed 1H–31P–31P correlation NMR spectroscopy techniques for the direct characterization of crude MEP pathway enzyme products at low concentrations (200 μM to 5 mM) on a room temperature (non-cryogenic) NMR probe. Coupling the 100% natural abundance of the 31P nucleus with the high intrinsic sensitivity of proton NMR, 1H–31P–31P correlation spectroscopy is particularly useful for characterization of unnatural diphosphate enzyme products in the MEP pathway. As proof of principle, we demonstrate the rapid characterization of natural enzyme products of the enzymes IspD, E and F in tandem enzyme incubations. In addition, we have characterized several unnatural enzyme products using this technique, including new products of cytidyltransferase IspD bearing erythritol, glycerol and ribose components. The results of this study indicate that IspD may be a useful biocatalyst and highlight 1H–31P–31P correlation spectroscopy as a valuable tool for the characterization of other unnatural products in non-mammalian isoprenoid biosynthesis.

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Probing phosphorylation by non-mammalian isoprenoid biosynthetic enzymes using 1H–31P–31P correlation NMR spectroscopy

et al. 2009

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31P-1H correlation and resonance assignments along the DNA backbone: three-dimensional implementation of heteronuclear long-range correlation experiment

Cited by 1 publication

References 31 publications

Probing phosphorylation by non-mammalian isoprenoid biosynthetic enzymes using 1H–31P–31P correlation NMR spectroscopy

Probing phosphorylation by non-mammalian isoprenoid biosynthetic enzymes using 1H–31P–31P correlation NMR spectroscopy

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