Related ArticlesCobalt(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 be replaced with Co2+ and Cu2+ to afford metal-substituted derivatives. Two Cu2+-substituted derivatives are detected by means of 1H NMR spectroscopy, a 'transient' derivative and a 'stable' derivative. The detection of sharp hyperfine-shifted 1H NMR signals in the 'transient' derivative indicates the formation of a magnetically coupled di-Cu2+ center, which concludes that the Zn2+ ions in the dinuclear (Zn1 and Zn3) sites are more easily replaced by Cu2+ than that in the Zn2 site. This might possibly be the case for Co2+ binding. Complete replacement of the three Zn2+ ions can be achieved by extensive dialysis of the enzyme against excess Cu2+ to yield the final 'stable' derivative. This derivative has been determined to have five-coordinated His residues and an overall S'=1/2 spin state with NMR and EPR, consistent with the formation of a tri-Cu2+ center (i.e. a di-Cu2+/mono-Cu2+ center) in this enzyme. The binding of substrate to the inert tri-Cu2+ center to form an enzyme-substrate (ES) complex is clearly seen in the 1H NMR spectrum, which is not obtainable in the case of the native enzyme. The change in the spectral features indicates that the substrate binds directly to the trinuclear metal center. The studies reported here suggest that 1H NMR spectroscopy can be a valuable tool for the characterization of di- and multi-nuclear metalloproteins using the 'NMR friendly' magnetically coupled Cu2+ as a probe.
Generation of Pseudocontact Shifts in Protein NMR Spectra with a Genetically Encoded Cobalt(II)-Binding Amino Acid.
Generation of Pseudocontact Shifts in Protein NMR Spectra with a Genetically Encoded Cobalt(II)-Binding Amino Acid.
Generation of Pseudocontact Shifts in Protein NMR Spectra with a Genetically Encoded Cobalt(II)-Binding Amino Acid.
Angew Chem Int Ed Engl. 2011 Jan 17;50(3):692-4
Authors: Nguyen TH, Ozawa K, Stanton-Cook M, Barrow R, Huber T, Otting G
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[NMR paper] A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domains.
A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domains.
Related Articles A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domains.
J Biol Chem. 2005 Nov 18;280(46):38259-63
Authors: Banci L, Bertini I, Cantini F, Chasapis CT, Hadjiliadis N, Rosato A
ATP7A is a P-type ATPase involved in copper(I) homeostasis in humans. It possesses a long N-terminal tail protruding into the cytosol and containing six...
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[NMR paper] Binding of copper(II) ions to the polyproline II helices of PEVK modules of the giant
Binding of copper(II) ions to the polyproline II helices of PEVK modules of the giant elastic protein titin as revealed by ESI-MS, CD, and NMR.
Related Articles Binding of copper(II) ions to the polyproline II helices of PEVK modules of the giant elastic protein titin as revealed by ESI-MS, CD, and NMR.
Biopolymers. 2003 Oct;70(3):297-309
Authors: Ma K, Wang K
Titin, a family of giant elastic proteins, constitutes an elastic sarcomere matrix in striated muscle. In the I-band region of the sarcomere, the titin PEVK segment acts as a molecular...
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NMR Characterization of Copper-Binding Domains 4-6 of ATP7B,
NMR Characterization of Copper-Binding Domains 4-6 of ATP7B,
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Biochemistry
DOI: 10.1021/bi1008535
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NMR Characterization of Copper-binding Domains 4-6 of ATP7B.
NMR Characterization of Copper-binding Domains 4-6 of ATP7B.
Related Articles NMR Characterization of Copper-binding Domains 4-6 of ATP7B.
Biochemistry. 2010 Aug 27;
Authors: Fatemi N, Korzhnev DM, VÄ?lyvis A, Sarkar B, Forman-Kay JD
The Wilson disease protein (ATP7B) is a copper-transporting member of the P-type ATPase superfamily, which plays a central role in copper homeostasis and interacts with the copper chaperone Atox1. The N-terminus of ATP7B is comprised of six copper-binding domains (WCBDs), each capable of binding one copper atom in the...
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[NMR paper] Paramagnetic NMR Spectroscopy of Cobalt(II) and Copper(II) Derivatives of Pseudomonas
Paramagnetic NMR Spectroscopy of Cobalt(II) and Copper(II) Derivatives of Pseudomonas aeruginosa His46Asp Azurin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Paramagnetic NMR Spectroscopy of Cobalt(II) and Copper(II) Derivatives of Pseudomonas aeruginosa His46Asp Azurin.
Inorg Chem. 1997 Sep 24;36(20):4567-4570
Authors: Vila AJ, Ramirez BE, Di Bilio AJ, Mizoguchi TJ, Richards JH, Gray HB
NMR spectra of paramagnetic Co(II) and Cu(II) derivatives of Pseudomonas aeruginosa His46Asp...
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[NMR paper] Structure and dynamics of the DNA binding protein HU from Bacillus stearothermophilus
Structure and dynamics of the DNA binding protein HU from Bacillus stearothermophilus by NMR spectroscopy.
Related Articles Structure and dynamics of the DNA binding protein HU from Bacillus stearothermophilus by NMR spectroscopy.
Biopolymers. 1996;40(5):553-9
Authors: Boelens R, Vis H, Vorgias CE, Wilson KS, Kaptein R
The DNA-binding protein HU from Bacillus stearothermophilus (HUBst) is a dimer with a molecular weight of 195 kDa that is capable of bending DNA. An x-ray structure has been determined previously , but no structure could be...
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[NMR paper] 1H-NMR study of a cobalt-substituted blue copper protein: Pseudomonas aeruginosa Co(I
1H-NMR study of a cobalt-substituted blue copper protein: Pseudomonas aeruginosa Co(II)-azurin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 1H-NMR study of a cobalt-substituted blue copper protein: Pseudomonas aeruginosa Co(II)-azurin.
Eur J Biochem. 1995 Jul 15;231(2):358-69
Authors: Salgado J, JimĂŠnez HR, Donaire A, Moratal JM
Substitution of copper by cobalt in blue copper proteins gives a paramagnetic metalloderivative...