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Rolff, Malte, Schottenheim, Julia, Decker, Heinz, Tuczek, Felix (2011) Copper–O2 reactivity of tyrosinase models towards external monophenolic substrates: molecular mechanism and comparison with the enzyme. Chemical Society Reviews, 40. 4077pp. doi:10.1039/c0cs00202j

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Reference TypeJournal (article/letter/editorial)
TitleCopper–O2 reactivity of tyrosinase models towards external monophenolic substrates: molecular mechanism and comparison with the enzyme
JournalChemical Society Reviews
AuthorsRolff, MalteAuthor
Schottenheim, JuliaAuthor
Decker, HeinzAuthor
Tuczek, FelixAuthor
Year2011Volume40
PublisherRoyal Society of Chemistry (RSC)
DOIdoi:10.1039/c0cs00202jSearch in ResearchGate
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Mindat Ref. ID4529893Long-form Identifiermindat:1:5:4529893:8
GUID0
Full ReferenceRolff, Malte, Schottenheim, Julia, Decker, Heinz, Tuczek, Felix (2011) Copper–O2 reactivity of tyrosinase models towards external monophenolic substrates: molecular mechanism and comparison with the enzyme. Chemical Society Reviews, 40. 4077pp. doi:10.1039/c0cs00202j
Plain TextRolff, Malte, Schottenheim, Julia, Decker, Heinz, Tuczek, Felix (2011) Copper–O2 reactivity of tyrosinase models towards external monophenolic substrates: molecular mechanism and comparison with the enzyme. Chemical Society Reviews, 40. 4077pp. doi:10.1039/c0cs00202j
In(2011) Chemical Society Reviews Vol. 40. Royal Society of Chemistry (RSC)

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Rolff, Malte, Schottenheim, Julia, Peters, Gerhard, Tuczek, Felix (2010) The First Catalytic Tyrosinase Model System Based on a Mononuclear Copper(I) Complex: Kinetics and Mechanism. Angewandte Chemie International Edition, 49 (36). 6438-6442 doi:10.1002/anie.201000973
Rolff, Malte, Schottenheim, Julia, Peters, Gerhard, Tuczek, Felix (2010) Das erste katalytische Tyrosinasemodell basierend auf einem einkernigen Kupfer(I)-Komplex: Kinetik und Mechanismus. Angewandte Chemie, 122 (36). 6583-6587 doi:10.1002/ange.201000973
Hamann, Jessica Nadine, Rolff, Malte, Tuczek, Felix (2015) Monooxygenation of an appended phenol in a model system of tyrosinase: implications on the enzymatic reaction mechanism. Dalton Transactions, 44 (7). 3251-3258 doi:10.1039/c4dt03010a
Schottenheim, Julia, Gernert, Claus, Herzigkeit, Benjamin, Krahmer, Jan, Tuczek, Felix (2015) Catalytic Models of Tyrosinase: Reactivity Differences between Systems Based on Mono- and Binucleating Ligands. European Journal of Inorganic Chemistry, 2015 (21) 3501-3511 doi:10.1002/ejic.201500029
Rolff, Malte, Tuczek, Felix (2008) How Do Copper Enzymes Hydroxylate Aliphatic Substrates? Recent Insights from the Chemistry of Model Systems. Angewandte Chemie International Edition, 47 (13). 2344-2347 doi:10.1002/anie.200705533
Decker, Heinz, Solem, Even, Tuczek, Felix (2018) Are glutamate and asparagine necessary for tyrosinase activity of type-3 copper proteins?. Inorganica Chimica Acta, 481. 32-37 doi:10.1016/j.ica.2017.11.031
Schottenheim, Julia, Fateeva, Natalie, Thimm, Wulf, Krahmer, Jan, Tuczek, Felix (2013) Catalytic Conversion of Monophenols toOrtho-Quinones in a Tyrosinase-Like Fashion: Towards More Biomimetic and More Efficient Model Systems. Zeitschrift für anorganische und allgemeine Chemie, 639. 1491-1497 doi:10.1002/zaac.201300065
Sander, Ole, Näther, Christian, Tuczek, Felix (2009) Chiral Dicopper Complexes with a Doubly Asymmetric Ligand as Models for the Tyrosinase Active Site: Synthesis, Structure, O2-Reactivity and Comparison with Their Symmetric Analogs. Zeitschrift für anorganische und allgemeine Chemie, 635. 1123-1133 doi:10.1002/zaac.200900095
Decker, Heinz, Schweikardt, Thorsten, Tuczek, Felix (2006) Die erste Kristallstruktur von Tyrosinase: alle Fragen beantwortet?. Angewandte Chemie, 118 (28). 4658-4663 doi:10.1002/ange.200601255
Solem, Even, Tuczek, Felix, Decker, Heinz (2016) Tyrosinase versus Catecholoxidase: ein Asparagin macht den Unterschied. Angewandte Chemie, 128 (8). 2934-2938 doi:10.1002/ange.201508534
Decker, Heinz, Schweikardt, Thorsten, Tuczek, Felix (2006) The First Crystal Structure of Tyrosinase: All Questions Answered?. Angewandte Chemie International Edition, 45 (28). 4546-4550 doi:10.1002/anie.200601255
 
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