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  1. Article ; Online: Mechanism of Radical Initiation in the Radical SAM Enzyme Superfamily.

    Hoffman, Brian M / Broderick, William E / Broderick, Joan B

    Annual review of biochemistry

    2023  Volume 92, Page(s) 333–349

    Abstract: ... ...

    Abstract Radical
    MeSH term(s) S-Adenosylmethionine/chemistry ; Iron-Sulfur Proteins/genetics ; Iron-Sulfur Proteins/chemistry
    Chemical Substances S-Adenosylmethionine (7LP2MPO46S) ; Iron-Sulfur Proteins
    Language English
    Publishing date 2023-04-04
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 207924-0
    ISSN 1545-4509 ; 0066-4154
    ISSN (online) 1545-4509
    ISSN 0066-4154
    DOI 10.1146/annurev-biochem-052621-090638
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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.209: Show issues Location:
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  2. Article ; Online: Impact of

    Whittington, Chris / Sharma, Ajay / Hill, S Gage / Iavarone, Anthony T / Hoffman, Brian M / Offenbacher, Adam R

    Biochemistry

    2024  

    Abstract: Lipoxygenases (LOXs) from pathogenic fungi are potential therapeutic targets for defense against plant and select human diseases. In contrast to the canonical LOXs in plants and animals, fungal LOXs are unique in having ... ...

    Abstract Lipoxygenases (LOXs) from pathogenic fungi are potential therapeutic targets for defense against plant and select human diseases. In contrast to the canonical LOXs in plants and animals, fungal LOXs are unique in having appended
    Language English
    Publishing date 2024-05-01
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/acs.biochem.4c00109
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  3. Article: Editorial: Animal Models in Psychiatry: Translating Animal Behavior to an Improved Understanding and Treatment of Psychiatric Disorders.

    Richtand, Neil M / Harvey, Brian H / Hoffman, Kurt Leroy

    Frontiers in psychiatry

    2022  Volume 13, Page(s) 876155

    Language English
    Publishing date 2022-03-24
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2564218-2
    ISSN 1664-0640
    ISSN 1664-0640
    DOI 10.3389/fpsyt.2022.876155
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  4. Article ; Online: Product analog binding identifies the copper active site of particulate methane monooxygenase.

    Tucci, Frank J / Jodts, Richard J / Hoffman, Brian M / Rosenzweig, Amy C

    Nature catalysis

    2023  Volume 6, Issue 12, Page(s) 1194–1204

    Abstract: Nature's primary methane-oxidizing enzyme, the membrane-bound particulate methane monooxygenase (pMMO), catalyzes the oxidation of methane to methanol. pMMO activity requires copper, and decades of structural and spectroscopic studies have sought to ... ...

    Abstract Nature's primary methane-oxidizing enzyme, the membrane-bound particulate methane monooxygenase (pMMO), catalyzes the oxidation of methane to methanol. pMMO activity requires copper, and decades of structural and spectroscopic studies have sought to identify the active site among three candidates: the Cu
    Language English
    Publishing date 2023-11-06
    Publishing country England
    Document type Journal Article
    ISSN 2520-1158
    ISSN (online) 2520-1158
    DOI 10.1038/s41929-023-01051-x
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  5. Article ; Online: Radical SAM enzymes: Nature's choice for radical reactions.

    Broderick, Joan B / Broderick, William E / Hoffman, Brian M

    FEBS letters

    2022  Volume 597, Issue 1, Page(s) 92–101

    Abstract: Enzymes that use a [4Fe-4S] ...

    Abstract Enzymes that use a [4Fe-4S]
    MeSH term(s) S-Adenosylmethionine/chemistry ; S-Adenosylmethionine/metabolism ; Iron-Sulfur Proteins/metabolism ; Enzymes/chemistry ; Enzymes/metabolism
    Chemical Substances S-Adenosylmethionine (7LP2MPO46S) ; Iron-Sulfur Proteins ; Enzymes
    Language English
    Publishing date 2022-10-27
    Publishing country England
    Document type Journal Article ; Review ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1002/1873-3468.14519
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.B 282: Show issues Location:
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  6. Article ; Online: ENDOR Spectroscopy Reveals the "Free" 5'-Deoxyadenosyl Radical in a Radical SAM Enzyme Active Site Actually is Chaperoned by Close Interaction with the Methionine-Bound [4Fe-4S]

    Yang, Hao / Ho, Madeline B / Lundahl, Maike N / Mosquera, Martín A / Broderick, William E / Broderick, Joan B / Hoffman, Brian M

    Journal of the American Chemical Society

    2024  Volume 146, Issue 6, Page(s) 3710–3720

    Abstract: ... 1/ ... ...

    Abstract 1/2
    MeSH term(s) S-Adenosylmethionine/metabolism ; Methionine ; Electron Spin Resonance Spectroscopy/methods ; Catalytic Domain ; Racemethionine ; Free Radicals/chemistry ; Iron-Sulfur Proteins/chemistry
    Chemical Substances S-Adenosylmethionine (7LP2MPO46S) ; Methionine (AE28F7PNPL) ; Racemethionine (73JWT2K6T3) ; Free Radicals ; Iron-Sulfur Proteins
    Language English
    Publishing date 2024-02-03
    Publishing country United States
    Document type Journal Article
    ZDB-ID 3155-0
    ISSN 1520-5126 ; 0002-7863
    ISSN (online) 1520-5126
    ISSN 0002-7863
    DOI 10.1021/jacs.3c09428
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  7. Article ; Online: Connecting the geometric and electronic structures of the nitrogenase iron-molybdenum cofactor through site-selective

    Badding, Edward D / Srisantitham, Suppachai / Lukoyanov, Dmitriy A / Hoffman, Brian M / Suess, Daniel L M

    Nature chemistry

    2023  Volume 15, Issue 5, Page(s) 658–665

    Abstract: Understanding the chemical bonding in the catalytic cofactor of the Mo nitrogenase (FeMo-co) is foundational for building a mechanistic picture of biological nitrogen fixation. A persistent obstacle towards this goal has been that ... ...

    Abstract Understanding the chemical bonding in the catalytic cofactor of the Mo nitrogenase (FeMo-co) is foundational for building a mechanistic picture of biological nitrogen fixation. A persistent obstacle towards this goal has been that the
    MeSH term(s) Nitrogenase/chemistry ; Molybdoferredoxin/chemistry ; Oxidation-Reduction ; Electron Spin Resonance Spectroscopy ; Catalysis
    Chemical Substances Nitrogenase (EC 1.18.6.1) ; Molybdoferredoxin
    Language English
    Publishing date 2023-03-13
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, N.I.H., Extramural
    ZDB-ID 2464596-5
    ISSN 1755-4349 ; 1755-4330
    ISSN (online) 1755-4349
    ISSN 1755-4330
    DOI 10.1038/s41557-023-01154-9
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  8. Article ; Online: Initial Steps in Methanobactin Biosynthesis: Substrate Binding by the Mixed-Valent Diiron Enzyme MbnBC.

    Jodts, Richard J / Ho, Madeline B / Reyes, Reyvin M / Park, Yun Ji / Doan, Peter E / Rosenzweig, Amy C / Hoffman, Brian M

    Biochemistry

    2024  

    Abstract: The MbnBC enzyme complex converts cysteine residues in a peptide substrate, MbnA, to oxazolone/thioamide groups during the biosynthesis of copper chelator methanobactin (Mbn). MbnBC belongs to the mixed-valent diiron oxygenase (MVDO) family, of which ... ...

    Abstract The MbnBC enzyme complex converts cysteine residues in a peptide substrate, MbnA, to oxazolone/thioamide groups during the biosynthesis of copper chelator methanobactin (Mbn). MbnBC belongs to the mixed-valent diiron oxygenase (MVDO) family, of which members use an Fe(II)Fe(III) cofactor to react with dioxygen for substrate modification. Several crystal structures of the inactive Fe(III)Fe(III) form of MbnBC alone and in complex with MbnA have been reported, but a mechanistic understanding requires determination of the oxidation states of the crystallographically observed Fe ions in the catalytically active Fe(II)Fe(III) state, along with the site of MbnA binding. Here, we have used electron nuclear double resonance (ENDOR) spectroscopy to determine such structural and electronic properties of the active site, in particular, the mode of substrate binding to the MV state, information not accessible by X-ray crystallography alone. The oxidation states of the two Fe ions were determined by
    Language English
    Publishing date 2024-04-08
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/acs.biochem.4c00011
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 217: Show issues Location:
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  9. Article ; Online: Pyruvate formate-lyase activating enzyme: The catalytically active 5'-deoxyadenosyl radical caught in the act of H-atom abstraction.

    Lundahl, Maike N / Yang, Hao / Broderick, William E / Hoffman, Brian M / Broderick, Joan B

    Proceedings of the National Academy of Sciences of the United States of America

    2023  Volume 120, Issue 47, Page(s) e2314696120

    Abstract: Enzymes of the ... ...

    Abstract Enzymes of the radical
    MeSH term(s) S-Adenosylmethionine/chemistry ; Acetyltransferases/metabolism ; Methionine ; Electron Spin Resonance Spectroscopy ; Peptides/metabolism ; Iron-Sulfur Proteins/metabolism
    Chemical Substances pyruvate formate-lyase activating enzyme (EC 2.3.1.-) ; S-Adenosylmethionine (7LP2MPO46S) ; Acetyltransferases (EC 2.3.1.-) ; Methionine (AE28F7PNPL) ; Peptides ; Iron-Sulfur Proteins
    Language English
    Publishing date 2023-11-13
    Publishing country United States
    Document type Journal Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2314696120
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    Zs.A 1148: Show issues Location:
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  10. Article ; Online: The Fe Protein Cycle Associated with Nitrogenase Catalysis Requires the Hydrolysis of Two ATP for Each Single Electron Transfer Event.

    Yang, Zhi-Yong / Badalyan, Artavazd / Hoffman, Brian M / Dean, Dennis R / Seefeldt, Lance C

    Journal of the American Chemical Society

    2023  Volume 145, Issue 10, Page(s) 5637–5644

    Abstract: A central feature of the current understanding of dinitrogen ( ... ...

    Abstract A central feature of the current understanding of dinitrogen (N
    MeSH term(s) Nitrogenase/chemistry ; Molybdoferredoxin/chemistry ; Electrons ; Hydrolysis ; Adenosine Triphosphate/chemistry ; Oxidation-Reduction ; Iron/metabolism ; Catalysis ; Electron Spin Resonance Spectroscopy
    Chemical Substances Nitrogenase (EC 1.18.6.1) ; Molybdoferredoxin ; Adenosine Triphosphate (8L70Q75FXE) ; Iron (E1UOL152H7)
    Language English
    Publishing date 2023-03-01
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 3155-0
    ISSN 1520-5126 ; 0002-7863
    ISSN (online) 1520-5126
    ISSN 0002-7863
    DOI 10.1021/jacs.2c09576
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