Literature DB >> 33409586

Fate of model complexes with monocopper center towards the functional properties of type 2 and type 3 copper oxidases.

Mariappan Murali1, Velusamy Sathya2, Balasubramaniam Selvakumaran2.   

Abstract

Green colored mononuclear copper(II) complexes viz. [Cu(L)(bpy)](ClO4) (1) or [Cu(L)(phen)](ClO4) (2) (where H(L) is 2-((2-dimethylamino)ethyliminomethyl)naphthol) show distorted square pyramidal (4 + 1) geometry with CuN4O chromophore. The existence of self-assembled molecular associations indicates the formation of the dimer. Dimeric nature in solution is retained due to the binding of the substrate, encourages steric match between substrate and Cu(II) active site, which favors electron transfer. Interestingly, both the complexes exhibit high-positive redox potential. Therefore, the presence of self-assembled molecular association along with the positive redox potential enhances the catalytic oxidation of ascorbic acid to dehydroascorbic acid or benzylamine to benaldehyde or catechol to o-quinone thereby model the functional properties of type 2 and type 3 copper oxidases. Notably, catalytic activity is effective when compared with other reported mononuclear copper(II) complexes and even superior to many binuclear copper(II) complexes. Existence of self-assembled molecular association in solution along with high-positive redox potential favors electron transfer process in mononuclear copper(II) complexes and models the functional properties of type 2 and type 3 copper oxidases.

Entities:  

Keywords:  Catalytic activity; Copper(II) complexes; Dimeric association; EPR sepctra; Redox potential

Year:  2021        PMID: 33409586     DOI: 10.1007/s00775-020-01837-5

Source DB:  PubMed          Journal:  J Biol Inorg Chem        ISSN: 0949-8257            Impact factor:   3.358


  24 in total

1.  Mechanisms Whereby Mononuclear Copper Proteins Functionalize Organic Substrates.

Authors:  Judith P. Klinman
Journal:  Chem Rev       Date:  1996-11-07       Impact factor: 60.622

2.  Multicopper Oxidases and Oxygenases.

Authors:  Edward I. Solomon; Uma M. Sundaram; Timothy E. Machonkin
Journal:  Chem Rev       Date:  1996-11-07       Impact factor: 60.622

Review 3.  Synthetic models of the active site of catechol oxidase: mechanistic studies.

Authors:  Iryna A Koval; Patrick Gamez; Catherine Belle; Katalin Selmeczi; Jan Reedijk
Journal:  Chem Soc Rev       Date:  2006-05-24       Impact factor: 54.564

4.  Theoretical study of the catalytic mechanism of catechol oxidase.

Authors:  Mireia Güell; Per E M Siegbahn
Journal:  J Biol Inorg Chem       Date:  2007-09-20       Impact factor: 3.358

Review 5.  Biologically inspired oxidation catalysis.

Authors:  Lawrence Que; William B Tolman
Journal:  Nature       Date:  2008-09-18       Impact factor: 49.962

Review 6.  Current challenges of modeling diiron enzyme active sites for dioxygen activation by biomimetic synthetic complexes.

Authors:  Simone Friedle; Erwin Reisner; Stephen J Lippard
Journal:  Chem Soc Rev       Date:  2010-05-20       Impact factor: 54.564

Review 7.  Copper-O2 reactivity of tyrosinase models towards external monophenolic substrates: molecular mechanism and comparison with the enzyme.

Authors:  Malte Rolff; Julia Schottenheim; Heinz Decker; Felix Tuczek
Journal:  Chem Soc Rev       Date:  2011-03-17       Impact factor: 54.564

8.  Kinetic and structural analysis of substrate specificity in two copper amine oxidases from Hansenula polymorpha.

Authors:  Cindy M Chang; Valerie J Klema; Bryan J Johnson; Minae Mure; Judith P Klinman; Carrie M Wilmot
Journal:  Biochemistry       Date:  2010-03-23       Impact factor: 3.162

9.  X-ray structures and mechanistic implications of three functional derivatives of ascorbate oxidase from zucchini. Reduced, peroxide and azide forms.

Authors:  A Messerschmidt; H Luecke; R Huber
Journal:  J Mol Biol       Date:  1993-04-05       Impact factor: 5.469

10.  Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution.

Authors:  M R Parsons; M A Convery; C M Wilmot; K D Yadav; V Blakeley; A S Corner; S E Phillips; M J McPherson; P F Knowles
Journal:  Structure       Date:  1995-11-15       Impact factor: 5.006

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