Related ArticlesNMR study of the exchange coupling in the trinuclear cluster of the multicopper oxidase fet3p.
J Am Chem Soc. 2010 Aug 18;132(32):11191-6
Authors: Zaballa ME, Ziegler L, Kosman DJ, Vila AJ
Fet3p from Saccharomyces cerevisiae is a multicopper oxidase (MCO) which oxidizes Fe(2+) to Fe(3+). The electronic structure of the different copper centers in this family of enzymes has been extensively studied and discussed for years with a particular focus on the exchange coupling regime in the trinuclear cluster (TNC). Using NMR spectroscopy we have quantified the exchange coupling constant in the type 3 center in a fully metalated oxidase; this value in Fet3p is significantly higher than that reported for proteins containing isolated type 3 centers as tyrosinase. We also provide evidence of exchange coupling between the type 2 and the type 3 Cu(2+) ions, which supports the crystallographic evidence of dioxygen binding to the TNC. This work provides the foundation for the application of NMR to these complex systems.
Longitudinal exchange: an alternative strategy towards quantification of dynamics parameters in ZZ exchange spectroscopy
Longitudinal exchange: an alternative strategy towards quantification of dynamics parameters in ZZ exchange spectroscopy
Abstract Longitudinal exchange experiments facilitate the quantification of the rates of interconversion between the exchanging species, along with their longitudinal relaxation rates, by analyzing the time-dependence of direct correlation and exchange cross peaks. Here we present a simple and robust alternative to this strategy, which is based on the combination of two complementary experiments, one with and one without resolving exchange cross peaks. We show that...
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[NMR paper] Cobalt(II) and copper(II) binding of Bacillus cereus trinuclear phospholipase C: a no
Cobalt(II) and copper(II) binding of Bacillus cereus trinuclear phospholipase C: a novel 1H NMR spectrum of a 'Tri-Cu(II)' center in protein.
Related Articles Cobalt(II) and copper(II) binding of Bacillus cereus trinuclear phospholipase C: a novel 1H NMR spectrum of a 'Tri-Cu(II)' center in protein.
J Inorg Biochem. 2001 Dec 1;87(3):149-56
Authors: Epperson JD, Ming LJ
The phosphatidylcholine-preferring phospholipase C from Bacillus cereus (PC-PLC(Bc)) is a tri-Zn enzyme with two 'tight binding' and one 'loose binding' sites. The Zn2+ ions can...
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11-19-2010 08:44 PM
NMR study of hydrogen exchange during the B-Z transition of a DNA duplex induced by t
NMR study of hydrogen exchange during the B-Z transition of a DNA duplex induced by the Z? domains of yatapoxvirus E3L.
Related Articles NMR study of hydrogen exchange during the B-Z transition of a DNA duplex induced by the Z? domains of yatapoxvirus E3L.
FEBS Lett. 2010 Oct 8;
Authors: Lee EH, Seo YJ, Ahn HC, Kang YM, Kim HE, Lee YM, Choi BS, Lee JH
The Yaba-like disease viruses (YLDV) are members of the Yatapoxvirus family and have double-stranded DNA genomes. The E3L protein, which is essential for pathogenesis in the vaccinia virus,...
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10-13-2010 02:18 PM
[NMR paper] A two-dimensional NMR study of exchange behavior of amide hydrogens in a lysozyme der
A two-dimensional NMR study of exchange behavior of amide hydrogens in a lysozyme derivative with an extra cross-link between Glu35 and Trp108--quenching of cooperative fluctuations and effects on the protein stability.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles A two-dimensional NMR study of exchange behavior of amide hydrogens in a lysozyme derivative with an extra cross-link between Glu35 and Trp108--quenching of cooperative fluctuations and effects on the protein...
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08-22-2010 03:31 PM
[NMR paper] A two-dimensional NMR study of exchange behavior of amide hydrogens in a lysozyme der
A two-dimensional NMR study of exchange behavior of amide hydrogens in a lysozyme derivative with an extra cross-link between Glu35 and Trp108--quenching of cooperative fluctuations and effects on the protein stability.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles A two-dimensional NMR study of exchange behavior of amide hydrogens in a lysozyme derivative with an extra cross-link between Glu35 and Trp108--quenching of cooperative fluctuations and effects on the protein...
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08-22-2010 03:03 PM
[NMR paper] Rapid corepressor exchange from the trp-repressor/operator complex: an NMR study of [
Rapid corepressor exchange from the trp-repressor/operator complex: an NMR study of -L-tryptophan.
Related Articles Rapid corepressor exchange from the trp-repressor/operator complex: an NMR study of -L-tryptophan.
J Biomol NMR. 1995 Jun;5(4):367-75
Authors: Lee W, Revington M, Farrow NA, Nakamura A, Utsunomiya-Tate N, Miyake Y, Kainosho M, Arrowsmith CH
-L-tryptophan was prepared biosynthetically and its dynamic properties and intermolecular interaction with a complex of Escherichia coli trp-repressor and a 20 base-pair operator DNA were...
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08-22-2010 03:41 AM
Suite of Six NMR Relaxation Dispersion Experiments to Study Multiple-Site Exchange in Proteins
http://pubs.acs.org/isubscribe/journals/jacsat/127/i44/figures/ja054550en00001.gif
Multiple-Site Exchange in Proteins Studied with a Suite of Six NMR Relaxation Dispersion Experiments: An Application to the Folding of a Fyn SH3 Domain Mutant
Dmitry M. Korzhnev, Philipp Neudecker, Anthony Mittermaier, Vladislav Yu. Orekhov, and Lewis E. Kay*
Contribution from the Departments of Medical Genetics, Biochemistry, and Chemistry, The University of Toronto, Toronto, Ontario M5S 1A8, Canada, and Swedish NMR Center at Göteborg University, Box 465, 405 30 Göteborg, Sweden
J. Am. Chem....
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01-12-2006 08:33 PM
15N SOFAST-HMQC to study fast H-D exchange
Very Fast Two-Dimensional NMR Spectroscopy for Real-Time Investigation of Dynamic Events in Proteins on the Time Scale of Seconds
Paul Schanda and Bernhard Brutscher
J. Am. Chem. Soc.; 2005; 127(22) pp 8014 - 8015
http://pubs.acs.org/isubscribe/journals/jacsat/127/i22/figures/ja051306en00001.gif
Abstract:
We demonstrate for different protein samples that 2D 1H-15N correlation NMR spectra can be recorded in a few seconds of acquisition time using a new band-selective optimized flip-angle short-transient heteronuclear multiple quantum coherence experiment. This has enabled us to...
NMR study of the exchange coupling in the trinuclear cluster of the multicopper oxida
Linear Mode
