1H, 15N and 13C backbone resonance assignments of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2-Reference-Cited by-同舟云学术

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1H, 15N and 13C backbone resonance assignments of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2

Published:2017-11-22 Issue:1 Volume:12 Page:79-83
ISSN:1874-2718
Container-title:Biomolecular NMR Assignments
language:en
Short-container-title:Biomol NMR Assign

Author:

Iorgu Andreea I.,Baxter Nicola J.,Cliff Matthew J.,Waltho Jonathan P.,Hay Sam,Scrutton Nigel S.^ORCID

Funder

European Union Seventh Framework Programme Marie Curie Initial Training Network MAGIC

Biotechnology and Biological Sciences Research Council

Engineering and Physical Sciences Research Council

Publisher

Springer Science and Business Media LLC

Subject

Biochemistry,Structural Biology

Link

http://link.springer.com/article/10.1007/s12104-017-9791-2/fulltext.html

Reference20 articles.

1. Barna TM, Khan H, Bruce NC et al (2001) Crystal structure of pentaerythritol tetranitrate reductase: “flipped” binding geometries for steroid substrates in different redox states of the enzyme. J Mol Biol 310:433–447. doi: 10.1006/jmbi.2001.4779

2. Basran J, Harris RJ, Sutcliffe MJ, Scrutton NS (2003) H-tunneling in the multiple H-transfers of the catalytic cycle of morphinone reductase and in the reductive half-reaction of the homologous pentaerythritol tetranitrate reductase. J Biol Chem 278:43973–43982. doi: 10.1074/jbc.M305983200

3. French CE, Nicklin S, Bruce NC (1996) Sequence and properties of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2. J Bacteriol 178:6623–6627. doi: 10.1128/jb.178.22.6623-6627.1996

4. Fryszkowska A, Toogood H, Sakuma M et al (2011) Active site modifications in pentaerythritol tetranitrate reductase can lead to improved product enantiopurity, decreased by-product formation and altered stereochemical outcome in reactions with α,β-unsaturated nitroolefins. Catal Sci Technol 1:948–957. doi: 10.1039/c0cy00092b

5. Gardner KH, Kay LE (1998) The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins. Annu Rev Biophys Biomol Struct 27:357–406. doi: 10.1146/annurev.biophys.27.1.357

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