Structural study of the X-ray-induced enzymatic reduction of molecular oxygen to water bySteccherinum murashkinskyilaccase: insights into the reaction mechanism

Serial crystallography captures enzyme catalysis in copper nitrite reductase at atomic resolution from one crystal

(2016) Sam Horrell et al.   IUCrJ

Three-dimensional structures of laccases

(2015) N. Hakulinen et al.   CELLULAR AND MOLECULAR LIFE SCIENCES

Electron transfer and reaction mechanism of laccases

(2015) Stephen M. Jones et al.   CELLULAR AND MOLECULAR LIFE SCIENCES

Structural insights into the O2reduction mechanism of multicopper oxidase

(2015) Hirofumi Komori et al.   JOURNAL OF BIOCHEMISTRY

Elucidation of the crystal structure ofCoriolopsis caperatalaccase: restoration of the structure and activity of the native enzyme from the T2-depleted form by copper ions

(2015) Olga A. Glazunova et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

X-ray-induced catalytic active-site reduction of a multicopper oxidase: structural insights into the proton-relay mechanism and O2-reduction states

(2015) Hugo Serrano-Posada et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Structural study of the X-ray-induced enzymatic reaction of octahaem cytochromecnitrite reductase

(2015) A. A. Trofimov et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Incorporation of copper ions into crystals of T2 copper-depleted laccase fromBotrytis aclada

(2015) E. M. Osipov et al.   Acta Crystallographica Section F-Structural Biology Communications

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

(2014) Hirofumi Komori et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Comparative analysis of the ligninolytic potential of basidiomycetes belonging to different taxonomic and ecological groups

(2013) T. V. Fedorova et al.   APPLIED BIOCHEMISTRY AND MICROBIOLOGY

Structural changes caused by radiation-induced reduction and radiolysis: the effect of X-ray absorbed dose in a fungal multicopper oxidase

(2012) Eugenio De la Mora et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

The role of Asp116 in the reductive cleavage of dioxygen to water in CotA laccase: assistance during the proton-transfer mechanism

(2012) Catarina S. Silva et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Analysis of copper–ligand bond lengths in X-ray structures of different types of copper sites in proteins

(2012) Luciano A. Abriata   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

An O-Centered Structure of the Trinuclear Copper Center in the Cys500Ser/Glu506Gln Mutant of CueO and Structural Changes in Low to High X-Ray Dose Conditions

(2012) Hirofumi Komori et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

Reaction intermediates and redox state changes in a blue laccase from Steccherinum ochraceum observed by crystallographic high/low X-ray dose experiments

(2012) Marta Ferraroni et al.   JOURNAL OF INORGANIC BIOCHEMISTRY

REFMAC5 for the refinement of macromolecular crystal structures

(2011) Garib N. Murshudov et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Overview of theCCP4 suite and current developments

(2011) Martyn D. Winn et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Coordination chemistry of copper proteins: How nature handles a toxic cargo for essential function

(2011) Jeffrey T. Rubino et al.   JOURNAL OF INORGANIC BIOCHEMISTRY

Optimization of data collection taking radiation damage into account

(2010) Gleb P. Bourenkov et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Radiation damage in macromolecular crystallography: what is it and why should we care?

(2010) Elspeth F. Garman   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

XDS

(2010) Wolfgang Kabsch   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Features and development ofCoot

(2010) P. Emsley et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Reductive cleavage of the O–O bond in multicopper oxidases: a QM/MM and QM study

(2010) Martin Srnec et al.   FARADAY DISCUSSIONS

Systematic Perturbation of the Trinuclear Copper Cluster in the Multicopper Oxidases: The Role of Active Site Asymmetry in Its Reduction of O2to H2O

(2010) Anthony J. Augustine et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Structure of native laccase fromTrametes hirsutaat 1.8 Å resolution

(2009) Konstantin M. Polyakov et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Laccases: a never-ending story

(2009) Paola Giardina et al.   CELLULAR AND MOLECULAR LIFE SCIENCES

Essential role of the C-terminus in Melanocarpus  albomyces laccase for enzyme production, catalytic properties and structure

(2009) Martina Andberg et al.   FEBS Journal

X-ray structure of a two-domain type laccase: A missing link in the evolution of multi-copper proteins

(2009) Hirofumi Komori et al.   FEBS LETTERS

Absorbed dose calculations for macromolecular crystals: improvements to RADDOSE

(2009) Karthik S. Paithankar et al.   JOURNAL OF SYNCHROTRON RADIATION

O2 Reduction to H2O by the multicopper oxidases

(2008) Edward I. Solomon et al.   DALTON TRANSACTIONS