ArticleActa crystallographica. Section D, Biological crystallography2015
X-ray-induced catalytic active-site reduction of a multicopper oxidase: structural insights into the proton-relay mechanism and O2-reduction states.
Article in Acta crystallographica. Section D, Biological crystallography, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed.
- Structure-Function Relationship of the β-Hairpin ofInternational journal of molecular sciences · 2025Article
- Biochemical and Structural Characterization of a Novel Psychrophilic Laccase (Multicopper Oxidase) Discovered fromInternational journal of molecular sciences · 2024Article
- Resonance Raman spectra of blue copper proteins: Variable temperature spectra of Thermus thermophilus HB27 laccase.Journal of inorganic biochemistry · 2023Article
- Laccase Engineering: Redox Potential Is Not the Only Activity-Determining Feature in the Metalloproteins.Molecules (Basel, Switzerland) · 2023Review
- Quantifying and comparing radiation damage in the Protein Data Bank.Nature communications · 2022Article
- The crucial role of bacterial laccases in the bioremediation of petroleum hydrocarbons.World journal of microbiology & biotechnology · 2020Review
- Chemical Exchange at the Trinuclear Copper Center of Small Laccase from Streptomyces coelicolor.Biophysical journal · 2020Article
- Stability/activity tradeoffs in Thermusthermophilus HB27 laccase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Article
- Investigations of Accessibility of T2/T3 Copper Center of Two-Domain Laccase fromInternational journal of molecular sciences · 2019Article
- Axial bonds at the T1 Cu site of Thermus thermophilus SG0.5JP17-16 laccase influence enzymatic properties.FEBS open bio · 2019Article
- Article
- Crystal structures of multicopper oxidase CueO G304K mutant: structural basis of the increased laccase activity.Scientific reports · 2018Article
- Living with Oxygen.Accounts of chemical research · 2018Article
- Crystal structure of CotA laccase complexed with 2,2-azinobis-(3-ethylbenzothiazoline-6-sulfonate) at a novel binding site.Acta crystallographica. Section F, Structural biology communications · 2016Article
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6 authors.
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Abstract
During X-ray data collection from a multicopper oxidase (MCO) crystal, electrons and protons are mainly released into the system by the radiolysis of water molecules, leading to the X-ray-induced reduction of O2 to 2H2O at the trinuclear copper cluster (TNC) of the enzyme. In this work, 12 crystallographic structures of Thermus thermophilus HB27 multicopper oxidase (Tth-MCO) in holo, apo and Hg-bound forms and with different X-ray absorbed doses have been determined. In holo Tth-MCO structures with four Cu atoms, the proton-donor residue Glu451 involved in O2 reduction was found in a double conformation: Glu451a (∼7 Å from the TNC) and Glu451b (∼4.5 Å from the TNC). A positive peak of electron density above 3.5σ in an Fo - Fc map for Glu451a O(ℇ2) indicates the presence of a carboxyl functional group at the side chain, while its significant absence in Glu451b strongly suggests a carboxylate functional group. In contrast, for apo Tth-MCO and in Hg-bound structures neither the positive peak nor double conformations were observed. Together, these observations provide the first structural evidence for a proton-relay mechanism in the MCO family and also support previous studies indicating that Asp106 does not provide protons for this mechanism. In addition, eight composite structures (Tth-MCO-C1-8) with different X-ray-absorbed doses allowed the observation of different O2-reduction states, and a total depletion of T2Cu at doses higher than 0.2 MGy showed the high susceptibility of this Cu atom to radiation damage, highlighting the importance of taking radiation effects into account in biochemical interpretations of an MCO structure.
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