Journal
BIOPHYSICAL JOURNAL
Volume 119, Issue 1, Pages 9-14Publisher
CELL PRESS
DOI: 10.1016/j.bpj.2020.05.022
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Funding
- Netherlands Magnetic Resonance Research School [NWO-BOO 022.005.029]
- Netherlands Organization for Scientific Research, Department of Chemical Sciences
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( )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 delta 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 g(z)-values. It is proposed that the exchange processes reflect the rotational motion of histidine imidazole rings that coordinate the coppers in the TNC.
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