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Using NMR solvent water relaxation to investigate metalloenzyme-ligand binding interactions.

Abstract:

This report demonstrates that solvent water relaxation measurements can be used for quantitative screening of ligand binding and for mechanistic investigations of enzymes containing paramagnetic metal centers by using conventional NMR instrumentation at high field. The method was exemplified using prolyl hydroxylase domain containing enzyme 2 (PHD2), a human enzyme involved in hypoxic sensing, with Mn(II) substituting for Fe(II) at the active site. K(D) values were determined for inhibitors t...

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Publication status:
Published

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Publisher copy:
10.1021/jm901537q

Authors


Flashman, E More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
Claridge, TD More by this author
Journal:
Journal of medicinal chemistry
Volume:
53
Issue:
2
Pages:
867-875
Publication date:
2010-01-05
DOI:
EISSN:
1520-4804
ISSN:
0022-2623
URN:
uuid:06b24475-be74-40ae-bc3b-9d5135434da9
Source identifiers:
35037
Local pid:
pubs:35037

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