Works (4)

Updated: September 12th, 2023 05:01

2023 journal article

A Ferric-Superoxide Intermediate Initiates P450-Catalyzed Cyclic Dipeptide Dimerization

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 8.

By: H. Gering n, X. Li n, H. Tang n, P. Swartz n, W. Chang n & T. Makris n

Sources: Web Of Science, NC State University Libraries, ORCID
Added: September 11, 2023

2021 article

BesC Initiates C-C Cleavage through a Substrate-Triggered and Reactive Diferric-Peroxo Intermediate

Manley, O. M., Tang, H., Xue, S., Guo, Y., Chang, W.-chen, & Makris, T. M. (2021, December 13). JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, Vol. 12.

By: O. Manley n, H. Tang n, S. Xue*, Y. Guo*, W. Chang n & T. Makris n

MeSH headings : Carbon / chemistry; Carbon / metabolism; Ferric Compounds / chemistry; Oxidoreductases / metabolism; Oxygen / chemistry; Spectroscopy, Mossbauer; Streptomyces / enzymology; Substrate Specificity
TL;DR: The observed reactivity of BesC represents the first example of a dinuclear-iron enzyme that utilizes a diferric-peroxo intermediate to capably cleave a C-H bond as part of its native function, thus circumventing the formation of a high-valent intermediate more commonly associated with substrate monooxygenations. (via Semantic Scholar)
UN Sustainable Development Goal Categories
Sources: Web Of Science, NC State University Libraries, ORCID
Added: January 3, 2022

2021 journal article

Harnessing the Substrate Promiscuity of Dioxygenase AsqJ and Developing Efficient Chemoenzymatic Synthesis for Quinolones

ACS CATALYSIS, 11(12), 7186–7192.

author keywords: Fe/2OG enzyme; AsqJ; chemoenzymatic synthesis; rearrangement; quinolone
TL;DR: By leveraging the power of chemo-enzymatic synthesis, a library of quinolone alkaloids is effectively prepared through chemoenzymatic cascades, and the robustness of this method in gram-scale reactions is evaluated. (via Semantic Scholar)
Sources: Web Of Science, NC State University Libraries
Added: July 19, 2021

2021 journal article

Mechanistic analysis of carbon-carbon bond formation by deoxypodophyllotoxin synthase

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 119(1).

By: H. Tang n, M. Wu*, H. Lin*, M. Han*, Y. Tu*, Z. Yang*, T. Chien*, N. Chan*, W. Chang n

author keywords: C-C coupling; cyclization; oxygenase; natural product; reaction mechanism
MeSH headings : Berberidaceae / enzymology; Drugs, Chinese Herbal / chemistry; Ligases / chemistry; Oxidation-Reduction; Plant Proteins / chemistry; Podophyllotoxin / analogs & derivatives; Podophyllotoxin / chemistry
TL;DR: This study reports two structures of DPS in complex with 2OG and (±)-yatein, in vitro analysis of enzymatic reactivity with substrate analogs, and model reactions addressing DPS’s catalytic mechanism, and suggests what types of substrate modification are likely tolerable in DPS-catalyzed production of deoxypodophyllotoxin analogs. (via Semantic Scholar)
Sources: Web Of Science, NC State University Libraries
Added: February 21, 2022

Citation Index includes data from a number of different sources. If you have questions about the sources of data in the Citation Index or need a set of data which is free to re-distribute, please contact us.

Certain data included herein are derived from the Web of Science© and InCites© (2024) of Clarivate Analytics. All rights reserved. You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.