Literature DB >> 8381679

Low frequency EPR of Pseudomonas aeruginosa azurin. Analysis of ligand superhyperfine structure from a type 1 copper site.

W E Antholine1, P M Hanna, D R McMillin.   

Abstract

The type 1 copper in Pseudomonas aeruginosa azurin was studied by electron paramagnetic resonance (EPR) spectroscopy at low microwave frequencies. Partially resolved ligand hyperfine structure was observed in the perpendicular region of the spectra at both S-band (2.4 GHz) and L-band (1.1 GHz). A trial and error method, requiring several hundred simulations, has been used to simulate the low frequency EPR data and yield an optimum value of 30 MHz for ACUx, more than one half that previously reported. The fit between the simulated and experimental data is sensitive to changes in the Euler angles and, in particular, to the angle alpha which rotates the Cu A-tensor about the z-axis. Thus, the A- and g-tensors for copper in P. aeruginosa azurin do not appear to be coincident. A value for the Euler angle beta of at least 10 degrees does not disturb the fit between the simulated and experimental data. These studies demonstrate the advantage of evaluating EPR parameters from simulations at more than one frequency, especially at low frequencies where ligand superhyperfine structure may be resolved for type 1 copper.

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Year:  1993        PMID: 8381679      PMCID: PMC1262323          DOI: 10.1016/S0006-3495(93)81363-8

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  11 in total

1.  EPR of azurins from Pseudomonas aeruginosa and Alcaligenes denitrificans demonstrates pH-dependence of the copper-site geometry in Pseudomonas aeruginosa protein.

Authors:  C M Groeneveld; R Aasa; B Reinhammar; G W Canters
Journal:  J Inorg Biochem       Date:  1987-10       Impact factor: 4.155

2.  Correlated distributions in g and A tensors at a biologically active low-symmetry cupric site.

Authors: 
Journal:  Phys Rev A       Date:  1991-10-15       Impact factor: 3.140

3.  A crystallographic model for azurin a 3 A resolution.

Authors:  E T Adman; R E Stenkamp; L C Sieker; L H Jensen
Journal:  J Mol Biol       Date:  1978-07-25       Impact factor: 5.469

4.  The amino acid sequence of Pseudomonas fluorescens azurin.

Authors:  R P Ambler; L H Brown
Journal:  Biochem J       Date:  1967-09       Impact factor: 3.857

5.  Kinetics of copper(II) uptake by apoazurin in complexing media.

Authors:  J A Blaszak; D R McMillin; A T Thornton; D L Tennent
Journal:  J Biol Chem       Date:  1983-08-25       Impact factor: 5.157

6.  Confirmation that multiexponential fluorescence decay behavior of holoazurin originates from conformational heterogeneity.

Authors:  C M Hutnik; A G Szabo
Journal:  Biochemistry       Date:  1989-05-02       Impact factor: 3.162

7.  Type 2-depleted fungal laccase.

Authors:  P M Hanna; D R McMillin; M Pasenkiewicz-Gierula; W E Antholine; B Reinhammar
Journal:  Biochem J       Date:  1988-07-15       Impact factor: 3.857

8.  X-ray crystal structure of the two site-specific mutants His35Gln and His35Leu of azurin from Pseudomonas aeruginosa.

Authors:  H Nar; A Messerschmidt; R Huber; M van de Kamp; G W Canters
Journal:  J Mol Biol       Date:  1991-03-20       Impact factor: 5.469

Review 9.  Copper protein structures.

Authors:  E T Adman
Journal:  Adv Protein Chem       Date:  1991

10.  Structure of azurin from Alcaligenes denitrificans refinement at 1.8 A resolution and comparison of the two crystallographically independent molecules.

Authors:  E N Baker
Journal:  J Mol Biol       Date:  1988-10-20       Impact factor: 5.469

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  7 in total

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

Authors:  Kyle M Lancaster; Stephen Sproules; Joshua H Palmer; John H Richards; Harry B Gray
Journal:  J Am Chem Soc       Date:  2010-10-20       Impact factor: 15.419

2.  Understanding the blue copper proteins.

Authors:  R L Belford
Journal:  Biophys J       Date:  1993-01       Impact factor: 4.033

3.  Uclacyanins, stellacyanins, and plantacyanins are distinct subfamilies of phytocyanins: plant-specific mononuclear blue copper proteins.

Authors:  A M Nersissian; C Immoos; M G Hill; P J Hart; G Williams; R G Herrmann; J S Valentine
Journal:  Protein Sci       Date:  1998-09       Impact factor: 6.725

4.  Outer-sphere contributions to the electronic structure of type zero copper proteins.

Authors:  Kyle M Lancaster; María-Eugenia Zaballa; Stephen Sproules; Mahesh Sundararajan; Serena DeBeer; John H Richards; Alejandro J Vila; Frank Neese; Harry B Gray
Journal:  J Am Chem Soc       Date:  2012-05-07       Impact factor: 15.419

5.  Modulating the Copper-Sulfur Interaction in Type 1 Blue Copper Azurin by Replacing Cys112 with Nonproteinogenic Homocysteine.

Authors:  Kevin M Clark; Yang Yu; Wilfred A van der Donk; Ninian Blackburn; Yi Lu
Journal:  Inorg Chem Front       Date:  2014-02-01       Impact factor: 6.569

6.  Temperature Dependence of Charge and Spin Transfer in Azurin.

Authors:  Yutao Sang; Suryakant Mishra; Francesco Tassinari; Senthil Kumar Karuppannan; Raanan Carmieli; Ruijie D Teo; Agostino Migliore; David N Beratan; Harry B Gray; Israel Pecht; Jonas Fransson; David H Waldeck; Ron Naaman
Journal:  J Phys Chem C Nanomater Interfaces       Date:  2021-04-29       Impact factor: 4.126

7.  Low-frequency EPR of ferrimyoglobin fluoride and ferrimyoglobin cyanide: a case study on the applicability of broadband analysis to high-spin hemoproteins and to HALS hemoproteins.

Authors:  Wilfred R Hagen
Journal:  J Biol Inorg Chem       Date:  2022-07-08       Impact factor: 3.862

  7 in total

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