Probing the dioxygen route in Melanocarpus albomyces laccase with pressurized xenon gas

J. P. Kallio, J. Rouvinen, Kristiina Kruus, N. Hakulinen (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

13 Citations (Scopus)

Abstract

Laccases catalyze the oxidation of phenolic substrates and the concominant reduction of dioxygen to water. We used xenon as an oxygen probe in search of routes for the entry of dioxygen into the catalytic center. Two xenon-pressurized crystal structures of recombinant Melanocarpus albomyces laccase were determined, showing three hydrophobic Xe-binding sites located in domain C. The analysis of hydrophobic cavities in other laccase structures further suggested the preference of domain C for binding of hydrophobic species such as dioxygen, thus suggesting that the hydrophobic core of domain C could function as a channel through which dioxygen can enter the trinuclear copper center.
Original languageEnglish
Pages (from-to)4396-4398
Number of pages3
JournalBiochemistry
Volume50
Issue number21
DOIs
Publication statusPublished - 2011
MoE publication typeA1 Journal article-refereed

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Laccase
Xenon
Gases
Oxygen
Copper
Crystal structure
Binding Sites
Oxidation
Water
Substrates

Cite this

Kallio, J. P. ; Rouvinen, J. ; Kruus, Kristiina ; Hakulinen, N. / Probing the dioxygen route in Melanocarpus albomyces laccase with pressurized xenon gas. In: Biochemistry. 2011 ; Vol. 50, No. 21. pp. 4396-4398.
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abstract = "Laccases catalyze the oxidation of phenolic substrates and the concominant reduction of dioxygen to water. We used xenon as an oxygen probe in search of routes for the entry of dioxygen into the catalytic center. Two xenon-pressurized crystal structures of recombinant Melanocarpus albomyces laccase were determined, showing three hydrophobic Xe-binding sites located in domain C. The analysis of hydrophobic cavities in other laccase structures further suggested the preference of domain C for binding of hydrophobic species such as dioxygen, thus suggesting that the hydrophobic core of domain C could function as a channel through which dioxygen can enter the trinuclear copper center.",
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Probing the dioxygen route in Melanocarpus albomyces laccase with pressurized xenon gas. / Kallio, J. P.; Rouvinen, J.; Kruus, Kristiina; Hakulinen, N. (Corresponding Author).

In: Biochemistry, Vol. 50, No. 21, 2011, p. 4396-4398.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Probing the dioxygen route in Melanocarpus albomyces laccase with pressurized xenon gas

AU - Kallio, J. P.

AU - Rouvinen, J.

AU - Kruus, Kristiina

AU - Hakulinen, N.

PY - 2011

Y1 - 2011

N2 - Laccases catalyze the oxidation of phenolic substrates and the concominant reduction of dioxygen to water. We used xenon as an oxygen probe in search of routes for the entry of dioxygen into the catalytic center. Two xenon-pressurized crystal structures of recombinant Melanocarpus albomyces laccase were determined, showing three hydrophobic Xe-binding sites located in domain C. The analysis of hydrophobic cavities in other laccase structures further suggested the preference of domain C for binding of hydrophobic species such as dioxygen, thus suggesting that the hydrophobic core of domain C could function as a channel through which dioxygen can enter the trinuclear copper center.

AB - Laccases catalyze the oxidation of phenolic substrates and the concominant reduction of dioxygen to water. We used xenon as an oxygen probe in search of routes for the entry of dioxygen into the catalytic center. Two xenon-pressurized crystal structures of recombinant Melanocarpus albomyces laccase were determined, showing three hydrophobic Xe-binding sites located in domain C. The analysis of hydrophobic cavities in other laccase structures further suggested the preference of domain C for binding of hydrophobic species such as dioxygen, thus suggesting that the hydrophobic core of domain C could function as a channel through which dioxygen can enter the trinuclear copper center.

U2 - 10.1021/bi200486b

DO - 10.1021/bi200486b

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VL - 50

SP - 4396

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