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International Union of Crystallography, Acta Crystallographica Section D: Biological Crystallography, 11(70), p. 2913-2923

DOI: 10.1107/s1399004714020380

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Effect of the L499M mutation of the ascomycetousBotrytis acladalaccase on redox potential and catalytic properties

Journal article published in 2014 by Evgeny Osipov, Konstantin Polyakov, Roman Kittl, Sergey Shleev ORCID, Pavel Dorovatovsky, Tamara Tikhonova, Stephan Hann ORCID, Roland Ludwig, Vladimir Popov
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

The structures of the ascomycetous B. aclada laccase and its L499M T1-site mutant have been solved at 1.7 Å resolution. The mutant enzyme shows a 140 mV lower redox potential of the type 1 copper and altered kinetic behaviour. The wild type and the mutant have very similar structures, which makes it possible to relate the changes in the redox potential to the L499M mutation