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Chemical Exchange at the Trinuclear Copper Center of Small Laccase from Streptomyces coelicolor.

ABSTRACT: The trinuclear copper center (TNC) of laccase reduces oxygen to water with very little overpotential. The arrangement of the coppers and ligands in the TNC is known to be from many crystal structures, yet information about possible dynamics of the ligands is absent. Here, we report dynamics at the TNC of small laccase from Streptomyces coelicolor using paramagnetic NMR and electron paramagnetic resonance spectroscopy. Fermi contact-shifted resonances tentatively assigned to histidine H?1 display a two-state chemical exchange with exchange rates in the order of 100 s-1. In the electron paramagnetic resonance spectra, at least two forms are observed with different gz-values. It is proposed that the exchange processes reflect the rotational motion of histidine imidazole rings that coordinate the coppers in the TNC.

SUBMITTER: Dasgupta R

PROVIDER: S-EPMC7335907 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature

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Chemical Exchange at the Trinuclear Copper Center of Small Laccase from Streptomyces coelicolor.

Dasgupta Rubin R Gupta Karthick B S S KBSS Nami Faezeh F de Groot Huub J M HJM Canters Gerard W GW Groenen Edgar J J EJJ Ubbink Marcellus M

Biophysical journal 20200529 1

The trinuclear copper center (TNC) of laccase reduces oxygen to water with very little overpotential. The arrangement of the coppers and ligands in the TNC is known to be from many crystal structures, yet information about possible dynamics of the ligands is absent. Here, we report dynamics at the TNC of small laccase from Streptomyces coelicolor using paramagnetic NMR and electron paramagnetic resonance spectroscopy. Fermi contact-shifted resonances tentatively assigned to histidine Hδ1 display ...[more]

PMID: 32531206

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