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  1. Article ; Online: Stabilizing Au

    Lindquist, Kurt P / Eghdami, Armin / Deschene, Christina R / Heyer, Alexander J / Wen, Jiajia / Smith, Alexander G / Solomon, Edward I / Lee, Young S / Neaton, Jeffrey B / Ryan, Dominic H / Karunadasa, Hemamala I

    Nature chemistry

    2023  Volume 15, Issue 12, Page(s) 1780–1786

    Abstract: ... Although ... ...

    Abstract Although Cu
    Language English
    Publishing date 2023-08-28
    Publishing country England
    Document type Journal Article
    ZDB-ID 2464596-5
    ISSN 1755-4349 ; 1755-4330
    ISSN (online) 1755-4349
    ISSN 1755-4330
    DOI 10.1038/s41557-023-01305-y
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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

    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
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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
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  4. 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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  5. 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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  6. Article: Frontier Molecular Orbital Contributions to Chlorination versus Hydroxylation Selectivity in the Non-Heme Iron Halogenase SyrB2

    Srnec, Martin / Solomon Edward I

    Journal of the American Chemical Society. 2017 Feb. 15, v. 139, no. 6

    2017  

    Abstract: ... was computationally evaluated for different substrates that had been studied experimentally. The Ï ... π-oriented relative to both the Cl– and the OH– ligands. From this ferric intermediate ... to rebound depending on the relative π-overlap with the substrate C radical. The differential contribution ...

    Abstract The ability of an FeᴵⱽO intermediate in SyrB2 to perform chlorination versus hydroxylation was computationally evaluated for different substrates that had been studied experimentally. The π-trajectory for H atom abstraction (FeᴵⱽO oriented perpendicular to the C–H bond of substrate) was found to lead to the S = 2 five-coordinate HO–Feᴵᴵᴵ–Cl complex with the C• of the substrate, π-oriented relative to both the Cl– and the OH– ligands. From this ferric intermediate, hydroxylation is thermodynamically favored, but chlorination is intrinsically more reactive due to the energy splitting between two key redox-active dπ* frontier molecular orbitals (FMOs). The splitting is determined by the differential ligand field effect of Cl– versus OH– on the Fe center. This makes chlorination effectively competitive with hydroxylation. Chlorination versus hydroxylation selectivity is then determined by the orientation of the substrate with respect to the HO–Fe–Cl plane that controls either the Cl– or the OH– to rebound depending on the relative π-overlap with the substrate C radical. The differential contribution of the two FMOs to chlorination versus hydroxylation selectivity in SyrB2 is related to a reaction mechanism that involves two asynchronous transfers: electron transfer from the substrate radical to the iron center followed by late ligand (Cl– or OH–) transfer to the substrate.
    Keywords chemical bonding ; chlorides ; chlorination ; electron transfer ; energy ; hydroxyl radicals ; hydroxylation ; iron ; ligands ; thermodynamics
    Language English
    Dates of publication 2017-0215
    Size p. 2396-2407.
    Publishing place American Chemical Society
    Document type Article
    ZDB-ID 3155-0
    ISSN 1520-5126 ; 0002-7863
    ISSN (online) 1520-5126
    ISSN 0002-7863
    DOI 10.1021%2Fjacs.6b11995
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  7. 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
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  8. 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
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  9. 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
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  10. Article: O2 Activation by Non-Heme Iron Enzymes

    Solomon, Edward I / Goudarzi Serra / Sutherlin Kyle D

    Biochemistry. 2016 Nov. 22, v. 55, no. 46

    2016  

    Abstract: ... of non-heme Fe enzymes generate high-spin FeᴵⱽO intermediates that provide both σ and π frontier ...

    Abstract The non-heme Fe enzymes are ubiquitous in nature and perform a wide range of functions involving O₂ activation. These had been difficult to study relative to heme enzymes; however, spectroscopic methods that provide significant insight into the correlation of structure with function have now been developed. This Current Topics article summarizes both the molecular mechanism these enzymes use to control O₂ activation in the presence of cosubstrates and the oxygen intermediates these reactions generate. Three types of O₂ activation are observed. First, non-heme reactivity is shown to be different from heme chemistry where a low-spin Feᴵᴵᴵ–OOH non-heme intermediate directly reacts with substrate. Also, two subclasses of non-heme Fe enzymes generate high-spin FeᴵⱽO intermediates that provide both σ and π frontier molecular orbitals that can control selectivity. Finally, for several subclasses of non-heme Fe enzymes, binding of the substrate to the Feᴵᴵ site leads to the one-electron reductive activation of O₂ to an Feᴵᴵᴵ-superoxide capable of H atom abstraction and electrophilic attack.
    Keywords enzymes ; heme ; iron ; oxygen ; spectral analysis
    Language English
    Dates of publication 2016-1122
    Size p. 6363-6374.
    Publishing place American Chemical Society
    Document type Article
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021%2Facs.biochem.6b00635
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