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  1. Article ; Online: New mechanistic insights into coupled binuclear copper monooxygenases from the recent elucidation of the ternary intermediate of tyrosinase.

    Kipouros, Ioannis / Solomon, Edward I

    FEBS letters

    2022  Volume 597, Issue 1, Page(s) 65–78

    Abstract: Tyrosinase is the most predominant member of the coupled binuclear copper (CBC) protein family. The recent trapping and spectroscopic definition of the elusive catalytic ternary intermediate (enzyme/ ... ...

    Abstract Tyrosinase is the most predominant member of the coupled binuclear copper (CBC) protein family. The recent trapping and spectroscopic definition of the elusive catalytic ternary intermediate (enzyme/O
    MeSH term(s) Monophenol Monooxygenase/chemistry ; Monophenol Monooxygenase/metabolism ; Copper/metabolism ; Mixed Function Oxygenases/metabolism ; Phenols ; Catalytic Domain ; Oxygen/metabolism
    Chemical Substances Monophenol Monooxygenase (EC 1.14.18.1) ; Copper (789U1901C5) ; Mixed Function Oxygenases (EC 1.-) ; Phenols ; Oxygen (S88TT14065)
    Language English
    Publishing date 2022-10-06
    Publishing country England
    Document type Journal Article ; Review ; Research Support, N.I.H., Extramural
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1002/1873-3468.14503
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: New mechanistic insights into coupled binuclear copper monooxygenases from the recent elucidation of the ternary intermediate of tyrosinase

    Kipouros, Ioannis / Solomon, Edward I.

    FEBS Letters. 2023 Jan., v. 597, no. 1 p.65-78

    2023  

    Abstract: Tyrosinase is the most predominant member of the coupled binuclear copper (CBC) protein family. The recent trapping and spectroscopic definition of the elusive catalytic ternary intermediate (enzyme/O₂/monophenol) of tyrosinase dictates a monooxygenation ...

    Abstract Tyrosinase is the most predominant member of the coupled binuclear copper (CBC) protein family. The recent trapping and spectroscopic definition of the elusive catalytic ternary intermediate (enzyme/O₂/monophenol) of tyrosinase dictates a monooxygenation mechanism that revises previous proposals and involves cleavage of the μ‐η²:η²‐peroxide dicopper(II) O–O bond to accept the phenolic proton, followed by monophenolate coordination to copper concomitant with aromatic hydroxylation by the non‐protonated μ‐oxo. Here, we compare and contrast previously proposed and current mechanistic models for monophenol monooxygenation of tyrosinase. Next, we discuss how these recent insights provide new opportunities towards uncovering structure–function relationships in CBC enzymes, as well as understanding fundamental principles for O₂ activation and reactivity by bioinorganic active sites.
    Keywords copper ; hydroxylation ; spectroscopy
    Language English
    Dates of publication 2023-01
    Size p. 65-78.
    Publishing place John Wiley & Sons, Ltd
    Document type Article ; Online
    Note REVIEW
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1002/1873-3468.14503
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  3. Article ; Online: Spiers Memorial Lecture: activating metal sites for biological electron transfer.

    Solomon, Edward I / Jose, Anex

    Faraday discussions

    2022  Volume 234, Page(s) 9–30

    Abstract: Metal sites in biology often exhibit unique spectroscopic features that reflect novel geometric and electronic structures imposed by the protein that are key to reactivity. The blue copper active site involved in long range, rapid biological electron ... ...

    Abstract Metal sites in biology often exhibit unique spectroscopic features that reflect novel geometric and electronic structures imposed by the protein that are key to reactivity. The blue copper active site involved in long range, rapid biological electron transfer is a classic example. This review presents an overview of both traditional and synchrotron based spectroscopic methods and their coupling to electronic structure calculations to understand the unique features of the blue copper active site, their contributions to function and the role of the protein in determining the geometric and electronic structure of the active site (called the "entatic state"). The relation of this active site to other biological electron transfer sites is further developed. In particular, ultrafast XFEL spectroscopy is used to evaluate the methionine-S-Fe bond in cytochrome
    MeSH term(s) Copper/chemistry ; Electron Transport ; Electrons ; Metals ; Models, Molecular
    Chemical Substances Metals ; Copper (789U1901C5)
    Language English
    Publishing date 2022-05-18
    Publishing country England
    Document type Journal Article ; Review ; Research Support, N.I.H., Extramural
    ISSN 1364-5498
    ISSN (online) 1364-5498
    DOI 10.1039/d2fd00001f
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Magnetic Exchange Coupling in Zeolite Copper Dimers and Its Contribution to Methane Activation.

    Heyer, Alexander J / Plessers, Dieter / Ma, Jing / Snyder, Benjamin E R / Schoonheydt, Robert A / Sels, Bert F / Solomon, Edward I

    Journal of the American Chemical Society

    2024  Volume 146, Issue 9, Page(s) 6061–6071

    Abstract: The highly reactive binuclear [ ... ...

    Abstract The highly reactive binuclear [Cu
    Language English
    Publishing date 2024-02-22
    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.3c13295
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Primary and Secondary Coordination Sphere Effects on the Structure and Function of

    Van Stappen, Casey / Dai, Huiguang / Jose, Anex / Tian, Shiliang / Solomon, Edward I / Lu, Yi

    Journal of the American Chemical Society

    2023  Volume 145, Issue 37, Page(s) 20610–20623

    Abstract: Much progress has been made in understanding the roles of the secondary coordination sphere (SCS) in tuning redox potentials of metalloproteins. In contrast, the impact of SCS on reactivity is much less understood. A primary example is how copper ... ...

    Abstract Much progress has been made in understanding the roles of the secondary coordination sphere (SCS) in tuning redox potentials of metalloproteins. In contrast, the impact of SCS on reactivity is much less understood. A primary example is how copper proteins can promote
    MeSH term(s) Azurin ; Copper ; Metalloproteins ; Catalysis ; Electronics
    Chemical Substances Azurin (12284-43-4) ; Copper (789U1901C5) ; Metalloproteins
    Language English
    Publishing date 2023-09-11
    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
    ZDB-ID 3155-0
    ISSN 1520-5126 ; 0002-7863
    ISSN (online) 1520-5126
    ISSN 0002-7863
    DOI 10.1021/jacs.3c07399
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Introductory lecture: general discussion.

    Dey, Abhishek / Goswami, Debabrata / Karlin, Kenneth / Solomon, Edward I / P Stack, T Daniel

    Faraday discussions

    2022  Volume 234, Page(s) 31–33

    Language English
    Publishing date 2022-05-18
    Publishing country England
    Document type Congress
    ISSN 1364-5498
    ISSN (online) 1364-5498
    DOI 10.1039/d2fd90011d
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: Geometric and Electronic Structural Contributions to Fe/O

    Solomon, Edward I / Iyer, Shyam R

    Bulletin of Japan Society of Coordination Chemistry

    2019  Volume 73, Page(s) 3–14

    Abstract: While two classes of non-heme iron enzymes use ferric centers to activate singlet organic substrates for the spin forbidden reaction ... ...

    Abstract While two classes of non-heme iron enzymes use ferric centers to activate singlet organic substrates for the spin forbidden reaction with
    Language English
    Publishing date 2019-05-31
    Publishing country Japan
    Document type Journal Article
    ISSN 1882-6954
    ISSN 1882-6954
    DOI 10.4019/bjscc.73.3
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Dioxygen Binding, Activation, and Reduction to H2O by Cu Enzymes.

    Solomon, Edward I

    Inorganic chemistry

    2016  Volume 55, Issue 13, Page(s) 6364–6375

    Abstract: Oxygen intermediates in copper enzymes exhibit unique spectroscopic features that reflect novel geometric and electronic structures that are key to reactivity. This perspective will describe: (1) the bonding origin of the unique spectroscopic features of ...

    Abstract Oxygen intermediates in copper enzymes exhibit unique spectroscopic features that reflect novel geometric and electronic structures that are key to reactivity. This perspective will describe: (1) the bonding origin of the unique spectroscopic features of the coupled binuclear copper enzymes and how this overcomes the spin forbiddenness of O2 binding and activates monooxygenase activity, (2) how the difference in exchange coupling in the non-coupled binuclear Cu enzymes controls the reaction mechanism, and (3) how the trinuclear Cu cluster present in the multicopper oxidases leads to a major structure/function difference in enabling the irreversible reductive cleavage of the O-O bond with little overpotential and generating a fully oxidized intermediate, different from the resting enzyme studied by crystallography, that is key in enabling fast PCET in the reductive half of the catalytic cycle.
    Language English
    Publishing date 2016-07-05
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1484438-2
    ISSN 1520-510X ; 0020-1669
    ISSN (online) 1520-510X
    ISSN 0020-1669
    DOI 10.1021/acs.inorgchem.6b01034
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  9. Article ; Online: Introduction: Oxygen Reduction and Activation in Catalysis.

    Solomon, Edward I / Stahl, Shannon S

    Chemical reviews

    2018  Volume 118, Issue 5, Page(s) 2299–2301

    Language English
    Publishing date 2018-03-13
    Publishing country United States
    Document type Editorial
    ZDB-ID 207949-5
    ISSN 1520-6890 ; 0009-2665
    ISSN (online) 1520-6890
    ISSN 0009-2665
    DOI 10.1021/acs.chemrev.8b00046
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: In Situ

    Bols, Max L / Ma, Jing / Rammal, Fatima / Plessers, Dieter / Wu, Xuejiao / Navarro-Jaén, Sara / Heyer, Alexander J / Sels, Bert F / Solomon, Edward I / Schoonheydt, Robert A

    Chemical reviews

    2024  Volume 124, Issue 5, Page(s) 2352–2418

    Abstract: This review ... ...

    Abstract This review highlights
    Language English
    Publishing date 2024-02-26
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 207949-5
    ISSN 1520-6890 ; 0009-2665
    ISSN (online) 1520-6890
    ISSN 0009-2665
    DOI 10.1021/acs.chemrev.3c00602
    Database MEDical Literature Analysis and Retrieval System OnLINE

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