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-Reference-Cited by-同舟云学术

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

Published:2011 Issue:6 Volume:1 Page:948
ISSN:2044-4753
Container-title:Catalysis Science & Technology
language:en
Short-container-title:Catal. Sci. Technol.

Author:

Fryszkowska Anna,Toogood Helen,Sakuma Michiyo,Stephens Gill M.,Gardiner John M.,Scrutton Nigel S.

Publisher

Royal Society of Chemistry (RSC)

Subject

Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2011/CY/C0CY00092B

Reference25 articles.

1. Crystal structure of pentaerythritol tetranitrate reductase: “flipped” binding geometries for steroid substrates in different redox states of the enzyme

2. Degradation of pentaerythritol tetranitrate by Enterobacter cloacae PB2

3. The Substrate Spectra of Pentaerythritol Tetranitrate Reductase, Morphinone Reductase,N-Ethylmaleimide Reductase and Estrogen-Binding Protein in the Asymmetric Bioreduction of Activated Alkenes

4. Sequence and properties of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2

5. Structure-Based Insight into the Asymmetric Bioreduction of the CC Double Bond of α,β-Unsaturated Nitroalkenes by Pentaerythritol Tetranitrate Reductase

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