The Protein’s Role in Substrate Positioning and Reactivity for Biosynthetic Enzyme Complexes: The Case of SyrB2/SyrB1-Reference-Cited by-同舟云学术

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The Protein’s Role in Substrate Positioning and Reactivity for Biosynthetic Enzyme Complexes: The Case of SyrB2/SyrB1

Published:2019-04-18 Issue:6 Volume:9 Page:4930-4943
ISSN:2155-5435
Container-title:ACS Catalysis
language:en
Short-container-title:ACS Catal.

Author:

Mehmood Rimsha,Qi Helena W.,Steeves Adam H.^ORCID,Kulik Heather J.^ORCID

Funder

National Institute of Environmental Health Sciences

Massachusetts Institute of Technology

U.S. Department of Energy

Burroughs Wellcome Fund

Publisher

American Chemical Society (ACS)

Subject

Catalysis,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acscatal.9b00865

Reference112 articles.

1. Non-Heme Fe(IV)–Oxo Intermediates

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

3. Fe(II)/α-Ketoglutarate-Dependent Hydroxylases and Related Enzymes

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

5. O2 Activation by Non-Heme Iron Enzymes

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1. Proton-triggered chemoselective halogenation of aliphatic C–H bonds with nonheme FeIV-oxo complexes;Journal of Inorganic Biochemistry;2024-10

2. Controllable Multihalogenation of a Non-native Substrate by the SyrB2 Iron Halogenase;ACS Catalysis;2024-08-19

3. Conformational Isomerization of the Fe(III)–OH Species Enables Selective Halogenation in Carrier-Protein-Independent Halogenase BesD and Hydroxylase-Evolved Halogenase;ACS Catalysis;2024-06-05

4. Controllable multi-halogenation of a non-native substrate by SyrB2 iron halogenase;2024-05-09

5. How Do Differences in Electronic Structure Affect the Use of Vanadium Intermediates as Mimics in Nonheme Iron Hydroxylases?;Inorganic Chemistry;2024-03-01

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