NDLI: Low-temperature magnetic circular dichroism studies of native laccase: spectroscopic evidence for exogenous ligand bridging at a trinuclear copper active site.

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Low-temperature magnetic circular dichroism studies of native laccase: spectroscopic evidence for exogenous ligand bridging at a trinuclear copper active site.

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Low-temperature magnetic circular dichroism studies of native laccase: spectroscopic evidence for exogenous ligand bridging at a trinuclear copper active site.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Allendorf, M. D. Spira, D. J. Solomon, E. I.
Abstract	The detailed nature of N-3 binding at the multi-copper active site in native laccase is investigated through a combination of low-temperature magnetic circular dichroism (LTMCD) and absorption spectroscopies. This combination of techniques allows charge-transfer spectral features associated with N-3 binding to the paramagnetic type 2 Cu(II) to be differentiated from those associated with binding to the antiferromagnetically coupled, and therefore diamagnetic, binuclear type 3 Cu(II) site. Earlier absorption titration studies have indicated that N-3 binds with two different binding constants, yielding a high-affinity and a low-affinity form. The studies presented here are interpreted as strong evidence that low-affinity N-3 bridges the paramagnetic type 2 and diamagnetic type 3 binuclear Cu(II) sites in fully oxidized laccase. This assignment is further supported by features in the MCD spectrum whose intensity correlates with an EPR signal associated with uncoupled type 3 Cu(II) sites. In these sites, N-3 has displaced the endogenous bridge, thereby rendering the site paramagnetic and detectable by both LTMCD and EPR spectroscopy. High-affinity N-3 is found to bind to the paramagnetic type 2 Cu(II) site in a limited fraction of the protein molecules that contains reduced type 3 sites. Finally, the possible role of this trinuclear (type 2-type 3) Cu(II) active site in enabling the irreversible reduction of dioxygen to water is considered.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	10
Volume Number	82
Language	English
Publisher	National Academy of Sciences
Publisher Date	1985-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Oxidoreductases Azides Pharmacology Binding Sites Cations, Divalent Circular Dichroism Copper Electron Spin Resonance Spectroscopy Laccase Ligands Models, Structural Plants Protein Conformation Spectrum Analysis Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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