Copper(I)‐Dioxygen Adducts and Copper Enzyme Mechanisms

Liu, Jeffrey J.; Díaz, Daniel E.; Quist, David A.; Karlin, Kenneth D.

doi:10.1002/ijch.201600025

Cited by 67 publications

(81 citation statements)

References 95 publications

(238 reference statements)

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“…While LPMOs have been studied less than other copper-containing monooxygenases, enzymatic and computational studies have led to the proposals of reaction mechanisms which may be similar to those suggested for PHM, DβM, and TβM; however, other possibilities exist [17, 77, 80–82]. Possible copper-(di)oxygen intermediates involved in HAT from substrate are shown in Fig.…”

Section: Single Copper Active Sitesmentioning

confidence: 96%

“…Reduction of O 2 using copper complexes and the subsequent reactivity of the resultant intermediates have both been widely studied [13–17]. Many different Cu n O 2 intermediates can be formed and have been extensively investigated in terms of spectroscopy and reactivity (Fig.…”

Section: Structurally Characterized Copper-dioxygen Speciesmentioning

confidence: 99%

“…Two crystal structures of cupric superoxide model complexes have since been reported, with superoxide binding either in an η 2 or η 1 fashion [32, 33]. The reactivity of cupric superoxide model complexes, as well as their importance in biology, has recently been reviewed [17]. Tolman and coworkers have published on other mononuclear high-valent copper-(di)oxygen intermediates, including side-on Cu III -peroxide and Cu III -hydroxide species [34, 35], the latter of which was found to be capable of performing oxidations of strong C–H bonds (BDE <99 kcal/mol) [36, 37].…”

Section: Structurally Characterized Copper-dioxygen Speciesmentioning

confidence: 99%

“…In the prevailing mechanism, it is thought that, following O 2 coordination and reduction at Cu M , a cupric superoxide is responsible for hydrogen atom transfer (HAT) from the substrate, resulting in a cupric hydroperoxide complex ( Hp ) and substrate radical [17]. The next step of the mechanism can go through two different paths.…”

Section: Single Copper Active Sitesmentioning

confidence: 99%

“…Multiple cupric superoxide complexes have been reported and characterized using a variety of spectroscopic techniques, including UV–Vis and resonance Raman (rR) spectroscopies [17, 62]. Substrate reactivity studies accompanied by mechanistic insights with model complexes have been reported by the groups of Karlin and Itoh.…”

Section: Single Copper Active Sitesmentioning

confidence: 99%

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Activation of dioxygen by copper metalloproteins and insights from model complexes

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Nature uses dioxygen as a key oxidant in the transformation of biomolecules. Among the enzymes that are utilized for these reactions are copper-containing met-alloenzymes, which are responsible for important biological functions such as the regulation of neurotransmitters, dioxygen transport, and cellular respiration. Enzymatic and model system studies work in tandem in order to gain an understanding of the fundamental reductive activation of dioxygen by copper complexes. This review covers the most recent advancements in the structures, spectroscopy, and reaction mechanisms for dioxygen-activating copper proteins and relevant synthetic models thereof. An emphasis has also been placed on cofactor biogenesis, a fundamentally important process whereby biomolecules are post-translationally modified by the pro-enzyme active site to generate cofactors which are essential for the catalytic enzymatic reaction. Significant questions remaining in copper-ion-mediated O2-activation in copper proteins are addressed.

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Section: Single Copper Active Sitesmentioning

confidence: 96%

Section: Structurally Characterized Copper-dioxygen Speciesmentioning

confidence: 99%

Section: Structurally Characterized Copper-dioxygen Speciesmentioning

confidence: 99%

Section: Single Copper Active Sitesmentioning

confidence: 99%

Section: Single Copper Active Sitesmentioning

confidence: 99%

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Activation of dioxygen by copper metalloproteins and insights from model complexes

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Impact of Intramolecular Hydrogen Bonding on the Reactivity of Cupric Superoxide Complexes with O−H and C−H Substrates

et al. 2019

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Impact of Intramolecular Hydrogen Bonding on the Reactivity of Cupric Superoxide Complexes with O−H and C−H Substrates

et al. 2019

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The dioxygen reactivity of as eries of TMPA-based copper(I) complexes (TMPA = tris(2-pyridylmethyl)amine), with and without secondary-coordination-sphere hydrogenbonding moieties,w as studied at À135 8 8Ci n2 -methyltetrahydrofuran (MeTHF). Kinetic stabilization of the H-bonded [( ðX 1 ÞðX 2 Þ TMPA)Cu II (O 2 C À )] + cupric superoxide species was achieved, and they were characterized by resonance Raman (rR) spectroscopy. The structures and physical properties of [( ðX 1 ÞðX 2 Þ TMPA)Cu II (N 3 À )] + azido analogues were compared, and the O 2 C À reactivity of ligand-Cu I complexes when an Hbonding moiety is replaced by amethyl group was contrasted. Ad rastic enhancement in the reactivity of the cupric superoxide towards phenolic substrates as well as oxidation of substrates possessing moderate C À Hb ond-dissociation energies is observed, correlating with the number and strength of the H-bonding groups.Oxidation and oxygenation reactions are vital for biological and synthetic processes. [1][2][3][4][5][6][7][8][9] In biology,s ome copper-containing metalloenzymes are capable of performing these reactions. [2,10] Forexample,galactose oxidase (GO) is responsible for the oxidation of primary alcohols to aldehydes (Figure 1A); monooxygenases such as peptidylglycine a-hydroxylating monooxygenase (PHM), dopamine b-monooxygenase (DbM), and lytic polysaccharide monooxygenases (LMPOs) catalytically hydroxylate organic substrates containing strong (85-100 kcal mol À1 )C ÀHb ond dissociation energies (BDEs) using dioxygen ( Figure 1B). [2,[10][11][12] These reactions are important for biosynthesis of human prohormones and neurotransmitters in the former,a nd breaking down polysaccharides in the latter. Acupric superoxide species (that is,Cu II À O 2 C À ,formed from the reaction of copper(I) and dioxygen) is postulated to be involved in the catalytic cycles of each of these enzymes. [11] In GO,t his complex abstracts ah ydrogen atom from anearby Tyrresidue,thereby forming the catalytically active intermediate responsible for substrate oxidation.While the exact nature of the reactive intermediate in LPMOs is still widely debated, [12][13][14] ac onsensus in the literature for PHM and DbMi sthat acupric superoxide is responsible for the initial hydrogen-atom transfer (HAT) from ac arbon substrate. [11] Thus,t he study of synthetic cupric superoxide model complexes to further understand their structures, physical-spectroscopic properties,a nd correlated reactivity toward the hydroxylation of substrates containing strong CÀ Hb onds is of considerable interest in catalysis.Ty pically,t hese primary copper-dioxygen superoxide model species [11,15,16] are difficult to study due to their tendency to form secondary Cu 2 -O 2 adducts (that is, m-1,2peroxo-dicopper(II), side-on peroxodicopper(II), or bis-moxodicopper(III) complexes) in solution. Researchers have been able to prevent the formation of 2:1C u:O 2 adducts through ligand design;the addition of as econdary coordination sphere of sterically bulky groups [17][18][19][20][21...

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Copper(I)‐Dioxygen Adducts and Copper Enzyme Mechanisms

Cited by 67 publications

References 95 publications

Activation of dioxygen by copper metalloproteins and insights from model complexes

Activation of dioxygen by copper metalloproteins and insights from model complexes

Impact of Intramolecular Hydrogen Bonding on the Reactivity of Cupric Superoxide Complexes with O−H and C−H Substrates

Impact of Intramolecular Hydrogen Bonding on the Reactivity of Cupric Superoxide Complexes with O−H and C−H Substrates

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