How Do Electrostatic Perturbations of the Protein Affect the Bifurcation Pathways of Substrate Hydroxylation versus Desaturation in the Nonheme Iron-Dependent Viomycin Biosynthesis Enzyme?-Reference-Cited by-同舟云学术

How Do Electrostatic Perturbations of the Protein Affect the Bifurcation Pathways of Substrate Hydroxylation versus Desaturation in the Nonheme Iron-Dependent Viomycin Biosynthesis Enzyme?

Published:2021-02-23 Issue:8 Volume:125 Page:1720-1737
ISSN:1089-5639
Container-title:The Journal of Physical Chemistry A
language:en
Short-container-title:J. Phys. Chem. A

Author:

Ali Hafiz Saqib¹²^ORCID,Henchman Richard H.¹²^ORCID,Warwicker Jim¹³,de Visser Sam P.¹⁴^ORCID

Affiliation:

1. Manchester Institute of Biotechnology, The University of Manchester, 131 Princess Street, Manchester M1 7DN, U.K.

2. Department of Chemistry, The University of Manchester, Oxford Road, Manchester M13 9PL, U.K.

3. School of Biological Sciences, Faculty of Biology, Medicine and Health, The University of Manchester, Oxford Road, Manchester M13 9PL, U.K.

4. Department of Chemical Engineering and Analytical Science, The University of Manchester, Oxford Road, Manchester M13 9PL, U.K.

Publisher

American Chemical Society (ACS)

Subject

Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jpca.1c00141

Reference125 articles.

1. Geometric and Electronic Structure/Function Correlations in Non-Heme Iron Enzymes

2. Oxygenases: mechanisms and structural motifs for O2 activation

3. Non-heme iron oxygenases

4. Dioxygen Activation at Mononuclear Nonheme Iron Active Sites: Enzymes, Models, and Intermediates

5. Reaction Mechanisms of Mononuclear Non-Heme Iron Oxygenases

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