167 related articles for article (PubMed ID: 34605435)
1. Crystal structures of a dodecameric multicopper oxidase from Marinithermus hydrothermalis.
Paavola JL; Battistin U; Ogata CM; Georgiadis MM
Acta Crystallogr D Struct Biol; 2021 Oct; 77(Pt 10):1336-1345. PubMed ID: 34605435
[TBL] [Abstract][Full Text] [Related]
2. Structural insights into the O2 reduction mechanism of multicopper oxidase.
Komori H; Higuchi Y
J Biochem; 2015 Oct; 158(4):293-8. PubMed ID: 26272825
[TBL] [Abstract][Full Text] [Related]
3. Basic and applied features of multicopper oxidases, CueO, bilirubin oxidase, and laccase.
Sakurai T; Kataoka K
Chem Rec; 2007; 7(4):220-9. PubMed ID: 17663447
[TBL] [Abstract][Full Text] [Related]
4. X-ray-induced catalytic active-site reduction of a multicopper oxidase: structural insights into the proton-relay mechanism and O2-reduction states.
Serrano-Posada H; Centeno-Leija S; Rojas-Trejo SP; Rodríguez-Almazán C; Stojanoff V; Rudiño-Piñera E
Acta Crystallogr D Biol Crystallogr; 2015 Dec; 71(Pt 12):2396-411. PubMed ID: 26627648
[TBL] [Abstract][Full Text] [Related]
5. Crystal structure of a blue laccase from Lentinus tigrinus: evidences for intermediates in the molecular oxygen reductive splitting by multicopper oxidases.
Ferraroni M; Myasoedova NM; Schmatchenko V; Leontievsky AA; Golovleva LA; Scozzafava A; Briganti F
BMC Struct Biol; 2007 Sep; 7():60. PubMed ID: 17897461
[TBL] [Abstract][Full Text] [Related]
6. Crystal structure of a two-domain multicopper oxidase: implications for the evolution of multicopper blue proteins.
Lawton TJ; Sayavedra-Soto LA; Arp DJ; Rosenzweig AC
J Biol Chem; 2009 Apr; 284(15):10174-80. PubMed ID: 19224923
[TBL] [Abstract][Full Text] [Related]
7. Structural and functional characterisation of multi-copper oxidase CueO from lignin-degrading bacterium Ochrobactrum sp. reveal its activity towards lignin model compounds and lignosulfonate.
Granja-Travez RS; Wilkinson RC; Persinoti GF; Squina FM; Fülöp V; Bugg TDH
FEBS J; 2018 May; 285(9):1684-1700. PubMed ID: 29575798
[TBL] [Abstract][Full Text] [Related]
8. Multicopper oxidases: modular structure, sequence space, and evolutionary relationships.
Gräff M; Buchholz PCF; Le Roes-Hill M; Pleiss J
Proteins; 2020 Oct; 88(10):1329-1339. PubMed ID: 32447824
[TBL] [Abstract][Full Text] [Related]
9. Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-A resolution containing a full complement of coppers.
Piontek K; Antorini M; Choinowski T
J Biol Chem; 2002 Oct; 277(40):37663-9. PubMed ID: 12163489
[TBL] [Abstract][Full Text] [Related]
10. New insights into the catalytic active-site structure of multicopper oxidases.
Komori H; Sugiyama R; Kataoka K; Miyazaki K; Higuchi Y; Sakurai T
Acta Crystallogr D Biol Crystallogr; 2014 Mar; 70(Pt 3):772-9. PubMed ID: 24598746
[TBL] [Abstract][Full Text] [Related]
11. Effect of the L499M mutation of the ascomycetous Botrytis aclada laccase on redox potential and catalytic properties.
Osipov E; Polyakov K; Kittl R; Shleev S; Dorovatovsky P; Tikhonova T; Hann S; Ludwig R; Popov V
Acta Crystallogr D Biol Crystallogr; 2014 Nov; 70(Pt 11):2913-23. PubMed ID: 25372682
[TBL] [Abstract][Full Text] [Related]
12. Amino acids located in the outer-sphere of the trinuclear copper center in a multicopper oxidase, CueO as the putative electron donor in the four-electron reduction of dioxygen.
Sakurai T; Yamamoto M; Ikeno S; Kataoka K
Biochim Biophys Acta Proteins Proteom; 2017 Aug; 1865(8):997-1003. PubMed ID: 28473295
[TBL] [Abstract][Full Text] [Related]
13. Elucidation of the crystal structure of Coriolopsis caperata laccase: restoration of the structure and activity of the native enzyme from the T2-depleted form by copper ions.
Glazunova OA; Polyakov KM; Fedorova TV; Dorovatovskii PV; Koroleva OV
Acta Crystallogr D Biol Crystallogr; 2015 Apr; 71(Pt 4):854-61. PubMed ID: 25849396
[TBL] [Abstract][Full Text] [Related]
14. Shall we dance? How a multicopper oxidase chooses its electron transfer partner.
Quintanar L; Stoj C; Taylor AB; Hart PJ; Kosman DJ; Solomon EI
Acc Chem Res; 2007 Jun; 40(6):445-52. PubMed ID: 17425282
[TBL] [Abstract][Full Text] [Related]
15. O
Sekretaryova A; Jones SM; Solomon EI
J Am Chem Soc; 2019 Jul; 141(28):11304-11314. PubMed ID: 31260290
[TBL] [Abstract][Full Text] [Related]
16. Crystal structure of a four-copper laccase complexed with an arylamine: insights into substrate recognition and correlation with kinetics.
Bertrand T; Jolivalt C; Briozzo P; Caminade E; Joly N; Madzak C; Mougin C
Biochemistry; 2002 Jun; 41(23):7325-33. PubMed ID: 12044164
[TBL] [Abstract][Full Text] [Related]
17. Mechanism of the reduction of the native intermediate in the multicopper oxidases: insights into rapid intramolecular electron transfer in turnover.
Heppner DE; Kjaergaard CH; Solomon EI
J Am Chem Soc; 2014 Dec; 136(51):17788-801. PubMed ID: 25490729
[TBL] [Abstract][Full Text] [Related]
18. 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; 2017 May; 73(Pt 5):388-401. PubMed ID: 28471364
[TBL] [Abstract][Full Text] [Related]
19. Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in Escherichia coli.
Roberts SA; Weichsel A; Grass G; Thakali K; Hazzard JT; Tollin G; Rensing C; Montfort WR
Proc Natl Acad Sci U S A; 2002 Mar; 99(5):2766-71. PubMed ID: 11867755
[TBL] [Abstract][Full Text] [Related]
20. Four second-sphere residues of Thermus thermophilus SG0.5JP17-16 laccase tune the catalysis by hydrogen-bonding networks.
Liu H; Zhu Y; Yang X; Lin Y
Appl Microbiol Biotechnol; 2018 May; 102(9):4049-4061. PubMed ID: 29516147
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
