“Yellow” laccase from Sclerotinia sclerotiorum is a blue laccase that enhances its substrate affinity by forming a reversible tyrosyl-product adduct

English version

Autoři: Augustin C. Mot ^aff001; Cristina Coman ^aff001; Niculina Hadade ^aff001; Grigore Damian ^aff004; Radu Silaghi-Dumitrescu ^aff001; Hendrik Heering ^aff003
Působiště autorů: Faculty of Chemistry and Chemical Engineering, Babes-Bolyai University, Cluj-Napoca, Romania ^aff001; Department of Biomolecular Physics, National Institute for Research and Development of Isotopic and Molecular Technologies, Cluj-Napoca, Romania ^aff002; Leiden Institute of Chemistry, Leiden University, Leiden, The Netherlands ^aff003; Faculty of Physics, Babes-Bolyai University, Cluj-Napoca, Romania ^aff004
Vyšlo v časopise: PLoS ONE 15(1)
Kategorie: Research Article
doi: https://doi.org/10.1371/journal.pone.0225530

Souhrn

Yellow laccases lack the typical blue type 1 Cu absorption band around 600 nm; however, multi-copper oxidases with laccase properties have been reported. We provide the first evidence that the yellow laccase isolated from Sclerotinia sclerotiorum is obtained from a blue form by covalent, but nevertheless reversible modification with a phenolic product. After separating the phenolics from the extracellular medium, a typical blue laccase is obtained. With ABTS as model substrate for this blue enzyme, a non-natural purple adduct is formed with a spectrum nearly identical to that of the 1:1 adduct of an ABTS radical and Tyr. This modification significantly increases the stability and substrate affinity of the enzyme, not by acting primarily as bound mediator, but by structural changes that also alters the type 1 Cu site. The HPLC-MS analyses of the ABTS adduct trypsin digests revealed a distinct tyrosine within a unique loop as site involved in the modification of the blue laccase form. Thus, S. sclerotiorum yellow laccase seems to be an intrinsically blue multi-copper oxidase that boosts its activity and stability with a radical-forming aromatic substrate. This particular case could, at least in part, explain the enigma of the yellow laccases.

Klíčová slova:

Electron spin resonance spectroscopy – Guanidines – Liquid chromatography-mass spectrometry – Oxidation-reduction reactions – Phenols – Tyrosine – Ultraviolet-visible spectroscopy – Laccases

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“Yellow” laccase from Sclerotinia sclerotiorum is a blue laccase that enhances its substrate affinity by forming a reversible tyrosyl-product adduct

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