Reactivity of the laccase trinuclear copper active site with dioxygen: an x-ray absorption edge study

Cole, James L.; Tan, Grace O.; Yang, E. K. L.; Hodgson, Keith O.; Solomon, Edward I.

doi:10.1021/ja00162a025

Cited by 84 publications

(81 citation statements)

References 3 publications

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“…Since contributions from each copper site overlap, the average copper-copper distance in the trinuclear copper center can be obtained. The EXAFS spectra of the type II copper-depleted laccase [73] and ascorbate oxidase [74] show that their type III coppers are in the cuprous state even under air and are therefore different from the coupled copper centers in hemocyanin and tyrosinase. The EXAFS spectrum of Cu A in N 2 OR was very similar to that of COX and a copper-copper distance of ca.…”

Section: X-ray Absorption Spectramentioning

confidence: 99%

Structure and function of type I copper in multicopper oxidases

Sakurai

Kataoka

2007

Cell. Mol. Life Sci.

132

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Abstract. The type I copper center in multicopper oxidases is constructed from 1Cys2His and weakly coordinating 1Met or the non-coordinating 1Phe/1Leu, and it exhibits spectral properties and an alkaline transition similar to those of the blue copper center in blue copper proteins. Since the type I copper center in multicopper oxidases is deeply buried inside the protein molecule, electron transfers to and from type I copper are performed through specific pathways: the hydrogen bond between an amino acid located at the substrate binding site and a His residue coordinating type I copper, and the His-Cys-His sequence connecting the type I copper center and the trinuclear copper center comprised of a type II copper and a pair of type III coppers. The intramolecular electron transfer rates can be tuned by mutating the fourth ligand of type I copper. Further, mutation at the Cys ligand gives a vacant type I copper center and traps the reaction intermediate during the four-electron reduction of dioxygen.

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Section: X-ray Absorption Spectramentioning

confidence: 99%

Structure and function of type I copper in multicopper oxidases

Sakurai

Kataoka

2007

Cell. Mol. Life Sci.

132

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“…Spektroskopijom kombinovanom sa kristalografijom dobijen je detaljni opis aktivnog mjesta lakaze. Magnetni cirkularni dihroizam (MCD) i apsorpciona spektroskopija X-zraka lakaze su pokazale da se Tip 2 i 3 centri kombinuju da bi funkcionisali kao trinuklearni bakarni klaster koji interaguje sa egzogenim ligandom ukljuĉujući reakciju sa dikiseonikom 1 (Cole et al, 1990). Tip 2 centar je 3-koordinovan sa dva histidinska liganda i vodom.…”

Section: Aktivno Mjesto Lakazeunclassified

“…Tip 3 bakar je 4 puta koordinovan i to sa tri histidina i premošćujućim hidoksidom (slika 1). Strukturni model premošćavanja izmeĊu Tipa 2 i 3 (slika 3A i 3B) (Cole et al, 1990;Palmer et al, 1999;Sundaran et al, 1997) je dao uvid u katalitiĉko redukovanje kiseonika do vode. Zakljuĉeno je da je bakar Tipa 2 neophodan za redukciju kiseonika, jer je premošćavanje do ovog centra ukljuĉeno u stabilizaciju peroksidnog intermedijera.…”

Section: Aktivno Mjesto Lakazeunclassified

“…U ovom Tip 2/3 modu nakon prve dvoelektronske redukcije peroksidni intermedijer omogućava drugu dvoelektronsku redukciju (od centara Tipa 2 i 1) tako što je peroksid direktno koordinovan za redukovani Tip 2 bakar, a redukovani Tip 1 bakar je kuplovan sa Tip 3 bakrom preko kovalentnih Cys-His veza (Clark i Solomon, 1992). U prethodnim studijama (Cole et al, 1990) pokazano je da 40% Tip 1 i Tip 3 centara koji reaguju sa dikiseonikom odgovara nativnoj lakazi (slika 3C). Oĉigledno je da je Tip 2 bakar neophodan za reaktivnost dikiseonika u lakazi i da se redukcija dikiseonika odigrava u odsustvu bakra Tipa 1.…”

Section: Aktivno Mjesto Lakazeunclassified

“…B. premošćavanje sva tri bakarna jona (modifikovano po Sunduran et al, 1997). C. Reaktivnost derivata lakaze sa kiseonikom (modifikovano po Cole et al, 1990).…”

Section: Aktivno Mjesto Lakazeunclassified

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Kupferproteine: Koordination und Aktivierung von Sauerstoff und seine Reduktion zu Wasser

Solomon¹,

Chen²,

Metz³

et al. 2001

Angew. Chem.

Self Cite

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Aktive Kupfer-und Eisenzentren dominieren das Gebiet der biologischen Sauerstoffchemie [1] und spielen wichtige Rollen in der homogenen [2] und der heterogenen Katalyse. [3,4] Kupferproteine sind an der reversiblen Disauerstoff-Koordination (H‰mocyanin), [5] an der mit der Oxidation von Substraten gekoppelten Zwei-Elektronen-Reduktion zu Peroxid (Amin-, Galactose-und Catechol-Oxidasen), [6] an der Aktivierung zur Hydroxylierung (Dopamin-b-Hydroxylase, Peptidylglycin-a-hydroxylierende Monooxygenase, Tyrosinase und partikul‰re Methan-Monooxygenase) [6,7] und an der mit der Substratoxidation einhergehenden Vier-Elektronen-Reduktion zu Wasser (Laccase, Ascorbat-Oxidase, Caeruloplasmin und Fet3p) [7] sowie an Protonen-Pumpen (Cytochrom-c-Oxidase, die auch H‰m-Eisenzentren enth‰lt) beteiligt. [8] Die bislang bekannten, an Disauerstoff-Koordination, -Aktivierung und -Reduktion beteiligten Kupferproteine sind, geordnet nach dem Strukturtyp des aktiven Zentrums, in [*] Prof.

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Reactivity of the laccase trinuclear copper active site with dioxygen: an x-ray absorption edge study

Cited by 84 publications

References 3 publications

Structure and function of type I copper in multicopper oxidases

Structure and function of type I copper in multicopper oxidases

Removal of phenols and dyes from wastewater using native and recombinant oxidative enzymes

Kupferproteine: Koordination und Aktivierung von Sauerstoff und seine Reduktion zu Wasser

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