4ner Citations

New insights into the catalytic active-site structure of multicopper oxidases.

Acta Crystallogr D Biol Crystallogr 70 772-9 (2014)
Related entries: 4e9v, 4e9w, 4e9x, 4e9y

Cited: 13 times
EuropePMC logo PMID: 24598746

Abstract

Structural models determined by X-ray crystallography play a central role in understanding the catalytic mechanism of enzymes. However, X-ray radiation generates hydrated electrons that can cause significant damage to the active sites of metalloenzymes. In the present study, crystal structures of the multicopper oxidases (MCOs) CueO from Escherichia coli and laccase from a metagenome were determined. Diffraction data were obtained from a single crystal under low to high X-ray dose conditions. At low levels of X-ray exposure, unambiguous electron density for an O atom was observed inside the trinuclear copper centre (TNC) in both MCOs. The gradual reduction of copper by hydrated electrons monitored by measurement of the Cu K-edge X-ray absorption spectra led to the disappearance of the electron density for the O atom. In addition, the size of the copper triangle was enlarged by a two-step shift in the location of the type III coppers owing to reduction. Further, binding of O2 to the TNC after its full reduction was observed in the case of the laccase. Based on these novel structural findings, the diverse resting structures of the MCOs and their four-electron O2-reduction process are discussed.

Articles - 4ner mentioned but not cited (1)

  1. Exogenous acetate ion reaches the type II copper centre in CueO through the water-excretion channel and potentially affects the enzymatic activity. Komori H, Kataoka K, Tanaka S, Matsuda N, Higuchi Y, Sakurai T. Acta Crystallogr F Struct Biol Commun 72 558-563 (2016)


Reviews citing this publication (4)

  1. Three-dimensional structures of laccases. Hakulinen N, Rouvinen J. Cell Mol Life Sci 72 857-868 (2015)
  2. Structural insights into the O2 reduction mechanism of multicopper oxidase. Komori H, Higuchi Y. J Biochem 158 293-298 (2015)
  3. Fungal Laccases: The Forefront of Enzymes for Sustainability. Loi M, Glazunova O, Fedorova T, Logrieco AF, Mulè G. J Fungi (Basel) 7 1048 (2021)
  4. A greener approach for resource recycling: Manganese bioleaching. Ghosh S, Mohanty S, Akcil A, Sukla LB, Das AP. Chemosphere 154 628-639 (2016)

Articles citing this publication (8)

  1. Structural study of the X-ray-induced enzymatic reduction of molecular oxygen to water by Steccherinum murashkinskyi laccase: insights into the reaction mechanism. Polyakov KM, Gavryushov S, Ivanova S, Fedorova TV, Glazunova OA, Popov AN, Koroleva OV. Acta Crystallogr D Struct Biol 73 388-401 (2017)
  2. Structural analysis and biochemical properties of laccase enzymes from two Pediococcus species. Olmeda I, Casino P, Collins RE, Sendra R, Callejón S, Huesa J, Soares AS, Ferrer S, Pardo I. Microb Biotechnol 14 1026-1043 (2021)
  3. Rat ceruloplasmin: a new labile copper binding site and zinc/copper mosaic. Samygina VR, Sokolov AV, Bourenkov G, Schneider TR, Anashkin VA, Kozlov SO, Kolmakov NN, Vasilyev VB. Metallomics 9 1828-1838 (2017)
  4. Redox Potential-Dependent Formation of an Unusual His-Trp Bond in Bilirubin Oxidase. Akter M, Tokiwa T, Shoji M, Nishikawa K, Shigeta Y, Sakurai T, Higuchi Y, Kataoka K, Shibata N. Chemistry 24 18052-18058 (2018)
  5. A new crystal form of Aspergillus oryzae catechol oxidase and evaluation of copper site structures in coupled binuclear copper enzymes. Penttinen L, Rutanen C, Saloheimo M, Kruus K, Rouvinen J, Hakulinen N. PLoS One 13 e0196691 (2018)
  6. Crystal structures of multicopper oxidase CueO G304K mutant: structural basis of the increased laccase activity. Wang H, Liu X, Zhao J, Yue Q, Yan Y, Gao Z, Dong Y, Zhang Z, Fan Y, Tian J, Wu N, Gong Y. Sci Rep 8 14252 (2018)
  7. Quantum Mechanical Study of Oxygen Ligands Protonation for the Stable States of the Laccase Active Site. Gavryushov S, Kuzmich NN, Polyakov KM. Int J Mol Sci 24 2990 (2023)
  8. From Gas Phase Observations to Solid State Reality: The Identification and Isolation of Trinuclear Salicylaldoximato Copper Complexes. Roach BD, Forgan RS, Kamenetzky E, Parsons S, Plieger PG, White FJ, Woodhouse S, Tasker PA. Molecules 27 6421 (2022)