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  1. Article ; Online: Seeing Is Believing: Advances in Biological Imaging.

    Zhang, Xin / Booker, Squire J

    ACS bio & med chem Au

    2024  Volume 4, Issue 1, Page(s) 1–3

    Language English
    Publishing date 2024-01-30
    Publishing country United States
    Document type Editorial
    ISSN 2694-2437
    ISSN (online) 2694-2437
    DOI 10.1021/acsbiomedchemau.3c00075
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Happy Birthday

    Booker, Squire J

    ACS bio & med chem Au

    2022  Volume 2, Issue 1, Page(s) 1–3

    Language English
    Publishing date 2022-02-16
    Publishing country United States
    Document type Editorial
    ISSN 2694-2437
    ISSN (online) 2694-2437
    DOI 10.1021/acsbiomedchemau.2c00006
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Happy Birthday ACS Bio & Med Chem Au!

    Squire J. Booker

    ACS Bio & Med Chem Au, Vol 2, Iss 1, Pp 1-

    2022  Volume 3

    Keywords Biology (General) ; QH301-705.5 ; Biochemistry ; QD415-436
    Language English
    Publishing date 2022-02-01T00:00:00Z
    Publisher American Chemical Society
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: Twenty Years of Radical SAM! The Genesis of the Superfamily.

    Booker, Squire J / Lloyd, Cody T

    ACS bio & med chem Au

    2022  Volume 2, Issue 6, Page(s) 538–547

    Language English
    Publishing date 2022-12-05
    Publishing country United States
    Document type Editorial
    ISSN 2694-2437
    ISSN (online) 2694-2437
    DOI 10.1021/acsbiomedchemau.2c00078
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Structural characterization of cobalamin-dependent radical S-adenosylmethionine methylases.

    Knox, Hayley L / Booker, Squire J

    Methods in enzymology

    2022  Volume 669, Page(s) 3–27

    Abstract: Cobalamin-dependent radical S-adenosylmethionine (SAM) methylases catalyze key steps in the biosynthesis of numerous biomolecules, including protein cofactors, antibiotics, herbicides, and other natural products, but have remained a relatively ... ...

    Abstract Cobalamin-dependent radical S-adenosylmethionine (SAM) methylases catalyze key steps in the biosynthesis of numerous biomolecules, including protein cofactors, antibiotics, herbicides, and other natural products, but have remained a relatively understudied subclass of radical SAM enzymes due to their inherent insolubility upon overproduction in Escherichia coli. These enzymes contain two cofactors: a [4Fe-4S] cluster that is ligated by three cysteine residues, and a cobalamin cofactor typically bound by residues in the N-terminal portion of the enzyme. Recent advances in the expression and purification of these enzymes in their active states and with both cofactors present has allowed for more detailed biochemical studies as well as structure determination by X-ray crystallography. Herein, we use KsTsrM and TokK to highlight methods for the structural characterization of cobalamin-dependent radical SAM (RS) enzymes and describe recent advances in in the overproduction and purification of these enzymes.
    MeSH term(s) Crystallography, X-Ray ; Escherichia coli/metabolism ; Methyltransferases/metabolism ; S-Adenosylmethionine/metabolism ; Vitamin B 12/metabolism
    Chemical Substances S-Adenosylmethionine (7LP2MPO46S) ; Methyltransferases (EC 2.1.1.-) ; Vitamin B 12 (P6YC3EG204)
    Language English
    Publishing date 2022-01-28
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, Non-U.S. Gov't
    ISSN 1557-7988
    ISSN (online) 1557-7988
    DOI 10.1016/bs.mie.2021.12.013
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Welcome to

    Booker, Squire J / Conway, Stuart J / Lavasanifar, Afsaneh

    ACS bio & med chem Au

    2021  Volume 1, Issue 1, Page(s) 1

    Language English
    Publishing date 2021-09-07
    Publishing country United States
    Document type Editorial
    ISSN 2694-2437
    ISSN (online) 2694-2437
    DOI 10.1021/acsbiomedchemau.1c00033
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Using peptide substrate analogs to characterize a radical intermediate in NosN catalysis.

    Wang, Bo / Silakov, Alexey / Booker, Squire J

    Methods in enzymology

    2022  Volume 666, Page(s) 469–487

    Abstract: Nosiheptide is a ribosomally produced and post-translationally modified thiopeptide antibiotic that displays potent antibacterial activity in vitro, especially against Gram-positive pathogens. It comprises a core peptide macrocycle that contains multiple ...

    Abstract Nosiheptide is a ribosomally produced and post-translationally modified thiopeptide antibiotic that displays potent antibacterial activity in vitro, especially against Gram-positive pathogens. It comprises a core peptide macrocycle that contains multiple thiazole rings, dehydrated serine and threonine residues, a tri-substituted 3-hydroxypyridine ring and several other modifications. Among these additional modifications includes a 3,4-dimethyl-2-indolic acid (DMIA) moiety that bridges Glu6 and Cys8 of the core peptide to form a second smaller ring system. This side-ring system is formed by the action of NosN, a radical S-adenosylmethionine (SAM) enzyme that falls within the class C radical SAM methylase (RSMT) family. However, the true function of NosN is to transfer a methylene group from the methyl moiety of SAM to C4 of 3-methylindolic acid (MIA) attached in a thioester linkage to Cys8 of the core peptide to set up a highly electrophilic species. This species is then trapped by the side chain of Glu6, resulting in formation of a lactone and the side-ring system. The NosN reaction requires two simultaneously bound molecules of SAM. The first, SAM
    MeSH term(s) Anti-Bacterial Agents ; Catalysis ; Iron-Sulfur Proteins/chemistry ; Methyltransferases/metabolism ; Peptides/chemistry ; S-Adenosylmethionine/metabolism
    Chemical Substances Anti-Bacterial Agents ; Iron-Sulfur Proteins ; Peptides ; S-Adenosylmethionine (7LP2MPO46S) ; Methyltransferases (EC 2.1.1.-)
    Language English
    Publishing date 2022-03-14
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ISSN 1557-7988
    ISSN (online) 1557-7988
    DOI 10.1016/bs.mie.2022.02.008
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: Enzymatic Fluoromethylation Enabled by the

    Neti, Syam Sundar / Wang, Bo / Iwig, David F / Onderko, Elizabeth L / Booker, Squire J

    ACS central science

    2023  Volume 9, Issue 5, Page(s) 905–914

    Abstract: Fluoromethyl, difluoromethyl, and trifluoromethyl groups are present in numerous pharmaceuticals and agrochemicals, where they play critical roles in the efficacy and metabolic stability of these molecules. Strategies for late-stage incorporation of ... ...

    Abstract Fluoromethyl, difluoromethyl, and trifluoromethyl groups are present in numerous pharmaceuticals and agrochemicals, where they play critical roles in the efficacy and metabolic stability of these molecules. Strategies for late-stage incorporation of fluorine-containing atoms in molecules have become an important area of organic and medicinal chemistry as well as synthetic biology. Herein, we describe the synthesis and use of
    Language English
    Publishing date 2023-05-08
    Publishing country United States
    Document type Journal Article
    ISSN 2374-7943
    ISSN 2374-7943
    DOI 10.1021/acscentsci.2c01385
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Welcome to ACS Bio & Med Chem Au

    Squire J. Booker / Stuart J. Conway / Afsaneh Lavasanifar

    ACS Bio & Med Chem Au, Vol 1, Iss 1, Pp 1-

    2021  Volume 1

    Keywords Biology (General) ; QH301-705.5 ; Biochemistry ; QD415-436
    Language English
    Publishing date 2021-09-01T00:00:00Z
    Publisher American Chemical Society
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  10. Article ; Online: The Expanding Role of Methyl-Coenzyme M Reductase in the Anaerobic Functionalization of Alkanes.

    Miller, Danielle V / Booker, Squire J

    Biochemistry

    2019  Volume 58, Issue 42, Page(s) 4269–4271

    MeSH term(s) Anaerobiosis ; Ethane/metabolism ; Hydrogen Bonding ; Methane/metabolism ; Methanosarcinales/genetics ; Methanosarcinales/metabolism ; Oxidation-Reduction ; Oxidoreductases/metabolism ; Phylogeny ; S-Adenosylmethionine/metabolism
    Chemical Substances S-Adenosylmethionine (7LP2MPO46S) ; Oxidoreductases (EC 1.-) ; methyl coenzyme M reductase (EC 2.8.4.1) ; Ethane (L99N5N533T) ; Methane (OP0UW79H66)
    Language English
    Publishing date 2019-10-11
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/acs.biochem.9b00859
    Database MEDical Literature Analysis and Retrieval System OnLINE

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