Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 4396-4398 |
| Number of pages | 3 |
| Journal | Biochemistry |
| Volume | 50 |
| Issue number | 21 |
| DOIs | |
| Publication status | Published - 2011 |
| MoE publication type | A1 Journal article-refereed |
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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 journal › Article › Scientific › peer-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
M3 - Article
VL - 50
SP - 4396
EP - 4398
JO - Biochemistry
JF - Biochemistry
SN - 0006-2960
IS - 21
ER -