1998
DOI: 10.1038/4193
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Crystal structure of a plant catechol oxidase containing a dicopper center

Abstract: Catechol oxidases are ubiquitous plant enzymes containing a dinuclear copper center. In the wound-response mechanism of the plant they catalyze the oxidation of a broad range of ortho-diphenols to the corresponding o-quinones coupled with the reduction of oxygen to water. The crystal structures of the enzyme from sweet potato in the resting dicupric Cu(II)-Cu(II) state, the reduced dicuprous Cu(I)-Cu(I) form, and in complex with the inhibitor phenylthiourea were analyzed. The catalytic copper center is accommo… Show more

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Cited by 824 publications
(827 citation statements)
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References 29 publications
(31 reference statements)
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“…These coacervates release the glue, which gelates in the sea water because of the lower solubility of Ca/Mg phosphate, and irreversible cysteine–DOPA cross‐links are formed (dopaquinones). This cross‐linking is catalysed through monophenoloxidase and catechol oxidase activity of a tyrosinase, which is present in the secretory cells (Solomon, Sundaram & Machonkin, 1996; Klabunde et al ., 1998; Wang & Stewart, 2013). …”
Section: Comparison Of Cement With Other Biological Adhesivesmentioning
confidence: 99%
“…These coacervates release the glue, which gelates in the sea water because of the lower solubility of Ca/Mg phosphate, and irreversible cysteine–DOPA cross‐links are formed (dopaquinones). This cross‐linking is catalysed through monophenoloxidase and catechol oxidase activity of a tyrosinase, which is present in the secretory cells (Solomon, Sundaram & Machonkin, 1996; Klabunde et al ., 1998; Wang & Stewart, 2013). …”
Section: Comparison Of Cement With Other Biological Adhesivesmentioning
confidence: 99%
“…Since the report on the crystal structure of catechol oxidase by Krebs and co-authors a few years ago, [1] the interest in model compounds of this biocatalyst, as well as for other type-3 copper enzymes (e.g., hemocyanin and tyrosinase) has taken a new turn. In particular, investigations on the substrate coordination to the copper centers, [2][3][4] the dioxygen activation and the subsequent reactivity of the peroxodicopper species, [5][6][7][8][9] and the role of a thioether linkage in a close proximity of the dicopper center, [10,11] found in catechol oxidase from Ipomoea batatas [1] and some hemocyanins [12,13] and tyrosinases, [14] have received a significant interest from the scientific community.…”
Section: Introductionmentioning
confidence: 99%
“…In particular, investigations on the substrate coordination to the copper centers, [2][3][4] the dioxygen activation and the subsequent reactivity of the peroxodicopper species, [5][6][7][8][9] and the role of a thioether linkage in a close proximity of the dicopper center, [10,11] found in catechol oxidase from Ipomoea batatas [1] and some hemocyanins [12,13] and tyrosinases, [14] have received a significant interest from the scientific community. Although there have been numerous reports on model complexes of catechol oxidase, detailed mechanistic studies on the catechol oxidation mechanism are unfortunately quite scarce, [15][16][17][18][19] and only in a few cases the mode of dioxygen reduction, for example, to dihydrogen peroxide or water, has been definitely established.…”
Section: Introductionmentioning
confidence: 99%
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