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Literature DB >> 20879734

Outer-sphere effects on reduction potentials of copper sites in proteins: the curious case of high potential type 2 C112D/M121E Pseudomonas aeruginosa azurin.

Kyle M Lancaster¹, Stephen Sproules, Joshua H Palmer, John H Richards, Harry B Gray.

Abstract

Redox and spectroscopic (electronic absorption, multifrequency electron paramagnetic resonance (EPR), and X-ray absorption) properties together with X-ray crystal structures are reported for the type 2 Cu(II) C112D/M121E variant of Pseudomonas aeruginosa azurin. The results suggest that Cu(II) is constrained from interaction with the proximal glutamate; this structural frustration implies a "rack" mechanism for the 290 mV (vs NHE) reduction potential measured at neutral pH. At high pH (∼9), hydrogen bonding in the outer coordination sphere is perturbed to allow axial glutamate ligation to Cu(II), with a decrease in potential to 119 mV. These results highlight the role played by outer-sphere interactions, and the structural constraints they impose, in determining the redox behavior of transition metal protein cofactors.

Entities: Chemical Disease Gene Mutation Species

Mesh：

Substances：
Azurin
Copper

Year: 2010 PMID： 20879734 PMCID： PMC3375907 DOI： 10.1021/ja105731x

Source DB: PubMed Journal: J Am Chem Soc ISSN： 0002-7863 Impact factor: 15.419

27 in total

1. Role of the axial ligand in type 1 Cu centers studied by point mutations of met148 in rusticyanin.

Authors: J F Hall; L D Kanbi; R W Strange; S S Hasnain
Journal: Biochemistry Date: 1999-09-28 Impact factor: 3.162

2. Metal-ligand interplay in blue copper proteins studied by 1H NMR spectroscopy: Cu(II)-pseudoazurin and Cu(II)-rusticyanin.

Authors: Antonio Donaire; Beatriz Jiménez; Claudio O Fernández; Roberta Pierattelli; Tomotake Niizeki; José-María Moratal; John F Hall; Takamitsu Kohzuma; S Samar Hasnain; Alejandro J Vila
Journal: J Am Chem Soc Date: 2002-11-20 Impact factor: 15.419

3. X-ray Absorption Spectra of the Oxidized and Reduced Forms of C112D Azurin from Pseudomonas aeruginosa.

Authors: Serena DeBeer; Cynthia N. Kiser; Gary A. Mines; John H. Richards; Harry B. Gray; Edward I. Solomon; Britt Hedman; Keith O. Hodgson
Journal: Inorg Chem Date: 1999-02-08 Impact factor: 5.165

4. Effect of pH and ligand binding on the structure of the Cu site of the Met121Glu mutant of azurin from Pseudomonas aeruginosa.

Authors: R W Strange; L M Murphy; B G Karlsson; B Reinhammar; S S Hasnain
Journal: Biochemistry Date: 1996-12-17 Impact factor: 3.162

5. Electronic characterization of the oxidized state of the blue copper protein rusticyanin by 1H NMR: is the axial methionine the dominant influence for the high redox potential?

Authors: A Donaire; B Jiménez; J Moratal; J F Hall; S S Hasnain
Journal: Biochemistry Date: 2001-01-23 Impact factor: 3.162

Outer-sphere effects on reduction potentials of copper sites in proteins: the curious case of high potential type 2 C112D/M121E Pseudomonas aeruginosa azurin.

1. Role of the axial ligand in type 1 Cu centers studied by point mutations of met148 in rusticyanin.

2. Metal-ligand interplay in blue copper proteins studied by 1H NMR spectroscopy: Cu(II)-pseudoazurin and Cu(II)-rusticyanin.

3. X-ray Absorption Spectra of the Oxidized and Reduced Forms of C112D Azurin from Pseudomonas aeruginosa.

4. Effect of pH and ligand binding on the structure of the Cu site of the Met121Glu mutant of azurin from Pseudomonas aeruginosa.

5. Electronic characterization of the oxidized state of the blue copper protein rusticyanin by 1H NMR: is the axial methionine the dominant influence for the high redox potential?

6. The role of hydrogen bonding at the active site of a cupredoxin: the Phe114Pro azurin variant.

7. Rack-induced metal binding vs. flexibility: Met121His azurin crystal structures at different pH.

8. The effect of iron-hexacyanide binding on the determination of redox potentials of cytochromes and copper proteins.

Review 9. Rack-induced bonding in blue-copper proteins.

10. pH dependence of the redox potential of Pseudomonas aeruginosa cytochrome c-551.

1. Flexibility of the metal-binding region in apo-cupredoxins.

Review 2. Protein design: toward functional metalloenzymes.

Review 3. Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.

4. Traversing the Red-Green-Blue Color Spectrum in Rationally Designed Cupredoxins.

5. Azurin as a protein scaffold for a low-coordinate nonheme iron site with a small-molecule binding pocket.

6. A Euclidean Perspective on the Unfolding of Azurin: Spatial Correlations.

7. Electron transfer reactivity of type zero Pseudomonas aeruginosa azurin.

Review 8. Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics.

9. Frustration Dynamics and Electron-Transfer Reorganization Energies in Wild-Type and Mutant Azurins.