Abstract
The non-haem Fe(II) and 2-oxoglutarate (2OG)-dependent oxygenases belong to a superfamily of structurally-related enzymes that play important biological roles in plants, microorganisms and animals. Structural, mechanistic and functional studies of 2OG oxygenases require efficient and effective biophysical tools. Nuclear magnetic resonance (NMR) spectroscopy is a useful tool to study this enzyme superfamily. It has been applied to obtain information about enzyme kinetics, identify and characterise 2OG oxygenase-catalysed oxidation products, elucidate the catalytic mechanism, monitor ligand binding and study protein dynamics. This review summarises the types of information that NMR spectroscopy can provide in the studies of 2OG oxygenases, highlights the advantages of the technique and describes its drawbacks.
PMID: 28893416 [PubMed - as supplied by publisher]
[NMR paper] Urea Dependent 15N NMR-Relaxation Studies on PfP2 Multimers Reveal that the C-Terminal Behaves like an Independent Intrinsically Disordered Peptide.
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Authors: Hosur RV
Abstract
Intrinsically disordered proteins or such domains in globular proteins are believed to be playing important roles in protein functions by virtue of their ability...
[NMR paper] Redox behaviour of the haem domain of flavocytochrome c3 from Shewanella frigidimarin
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FEBS Lett. 2004 Dec 3;578(1-2):185-90
Authors: Pessanha M, Rothery EL, Louro RO, Turner DL, Miles CS, Reid GA, Chapman SK, Xavier AV, Salgueiro CA
Flavocytochrome c3 from Shewanella frigidimarina (fcc3) is a tetrahaem periplasmic protein of 64 kDa with fumarate reductase activity. This work reports the first example of NMR...
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[NMR paper] NMR structure of the haem core of a novel tetrahaem cytochrome isolated from Shewanel
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FEBS Lett. 2001 Jan 26;489(1):8-13
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The tetrahaem cytochrome isolated...
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[NMR paper] Characterization of the haem environment in Methylophilus methylotrophus ferricytochr
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Two-dimensional NMR techniques have been used to assign proton resonances in the haem cavity of...
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[NMR paper] 1H- and 13C-NMR investigation of redox-state-dependent and temperature-dependent conf
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[NMR paper] NMR studies of the C-terminal secretion signal of the haem-binding protein, HasA.
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