Isomorphic deactivation of a Pseudomonas aeruginosa oxidoreductase: The crystal structure of Ag(I) metallated azurin at 1.7 Å

Matthew J. Panzner; Stephanie M. Bilinovich; Jillian A. Parker; Erika L. Bladholm; Christopher J. Ziegler; Steven M. Berry; Thomas C. Leeper

doi:10.1016/j.jinorgbio.2013.07.011

Isomorphic deactivation of a Pseudomonas aeruginosa oxidoreductase: The crystal structure of Ag(I) metallated azurin at 1.7 Å

Matthew J. Panzner, Stephanie M. Bilinovich, Jillian A. Parker, Erika L. Bladholm, Christopher J. Ziegler, Steven M. Berry, Thomas C. Leeper

Chemistry & Biochemistry

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

Abstract

Multiple biophysical methods demonstrate that silver effectively metallates Pseudomonas aeruginosa apo-azurin in solution. X-ray crystallography of the silver-modified protein reveals that silver binds to azurin at the traditional copper mediated active site with nearly identical geometry. Cyclic voltammetry indicates that the silver adduct is redox inert. Our results suggest that a potential mechanism for the microbial toxicity of silver is the deactivation of copper oxidoreductases by the effective binding and structural mimicry by silver without the corresponding function.

Original language	English (US)
Pages (from-to)	11-16
Number of pages	6
Journal	Journal of Inorganic Biochemistry
Volume	128
DOIs	https://doi.org/10.1016/j.jinorgbio.2013.07.011
State	Published - 2013

Bibliographical note

Funding Information:
This work was supported by The University of Akron . We wish to thank the National Science Foundation for funds used to purchase the Bruker Apex II Duo CCD X-ray diffractometer (CHE-0840446) used in this research. We thank the Kresge Foundation and donors to the Kresge Challenge Program at The University of Akron for funds used to purchase the NMR instrument used in this work. We also wish to thank the Center for Silver Therapeutics Research at The University of Akron. We thank the Swenson Family Foundation (UMD) for funding and student stipends. Finally, we would like to thank John H. Richards, California Institute of Technology, and Yi Lu of the University of Illinois at Urbana-Champaign for the kind gift of the azurin gene.

Keywords

Azurin
Crystallography
NMR
Silver ion

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10.1016/j.jinorgbio.2013.07.011

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title = "Isomorphic deactivation of a Pseudomonas aeruginosa oxidoreductase: The crystal structure of Ag(I) metallated azurin at 1.7 {\AA}",

abstract = "Multiple biophysical methods demonstrate that silver effectively metallates Pseudomonas aeruginosa apo-azurin in solution. X-ray crystallography of the silver-modified protein reveals that silver binds to azurin at the traditional copper mediated active site with nearly identical geometry. Cyclic voltammetry indicates that the silver adduct is redox inert. Our results suggest that a potential mechanism for the microbial toxicity of silver is the deactivation of copper oxidoreductases by the effective binding and structural mimicry by silver without the corresponding function.",

keywords = "Azurin, Crystallography, NMR, Silver ion",

author = "Panzner, {Matthew J.} and Bilinovich, {Stephanie M.} and Parker, {Jillian A.} and Bladholm, {Erika L.} and Ziegler, {Christopher J.} and Berry, {Steven M.} and Leeper, {Thomas C.}",

note = "Funding Information: This work was supported by The University of Akron . We wish to thank the National Science Foundation for funds used to purchase the Bruker Apex II Duo CCD X-ray diffractometer (CHE-0840446) used in this research. We thank the Kresge Foundation and donors to the Kresge Challenge Program at The University of Akron for funds used to purchase the NMR instrument used in this work. We also wish to thank the Center for Silver Therapeutics Research at The University of Akron. We thank the Swenson Family Foundation (UMD) for funding and student stipends. Finally, we would like to thank John H. Richards, California Institute of Technology, and Yi Lu of the University of Illinois at Urbana-Champaign for the kind gift of the azurin gene. ",

year = "2013",

doi = "10.1016/j.jinorgbio.2013.07.011",

language = "English (US)",

volume = "128",

pages = "11--16",

journal = "Journal of Inorganic Biochemistry",

issn = "0162-0134",

publisher = "Elsevier Inc.",

}

TY - JOUR

T1 - Isomorphic deactivation of a Pseudomonas aeruginosa oxidoreductase

T2 - The crystal structure of Ag(I) metallated azurin at 1.7 Å

AU - Panzner, Matthew J.

AU - Bilinovich, Stephanie M.

AU - Parker, Jillian A.

AU - Bladholm, Erika L.

AU - Ziegler, Christopher J.

AU - Berry, Steven M.

AU - Leeper, Thomas C.

N1 - Funding Information: This work was supported by The University of Akron . We wish to thank the National Science Foundation for funds used to purchase the Bruker Apex II Duo CCD X-ray diffractometer (CHE-0840446) used in this research. We thank the Kresge Foundation and donors to the Kresge Challenge Program at The University of Akron for funds used to purchase the NMR instrument used in this work. We also wish to thank the Center for Silver Therapeutics Research at The University of Akron. We thank the Swenson Family Foundation (UMD) for funding and student stipends. Finally, we would like to thank John H. Richards, California Institute of Technology, and Yi Lu of the University of Illinois at Urbana-Champaign for the kind gift of the azurin gene.

PY - 2013

Y1 - 2013

N2 - Multiple biophysical methods demonstrate that silver effectively metallates Pseudomonas aeruginosa apo-azurin in solution. X-ray crystallography of the silver-modified protein reveals that silver binds to azurin at the traditional copper mediated active site with nearly identical geometry. Cyclic voltammetry indicates that the silver adduct is redox inert. Our results suggest that a potential mechanism for the microbial toxicity of silver is the deactivation of copper oxidoreductases by the effective binding and structural mimicry by silver without the corresponding function.

AB - Multiple biophysical methods demonstrate that silver effectively metallates Pseudomonas aeruginosa apo-azurin in solution. X-ray crystallography of the silver-modified protein reveals that silver binds to azurin at the traditional copper mediated active site with nearly identical geometry. Cyclic voltammetry indicates that the silver adduct is redox inert. Our results suggest that a potential mechanism for the microbial toxicity of silver is the deactivation of copper oxidoreductases by the effective binding and structural mimicry by silver without the corresponding function.

KW - Azurin

KW - Crystallography

KW - NMR

KW - Silver ion

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AN - SCOPUS:84880912918

SN - 0162-0134

VL - 128

SP - 11

EP - 16

JO - Journal of Inorganic Biochemistry

JF - Journal of Inorganic Biochemistry

ER -

Isomorphic deactivation of a Pseudomonas aeruginosa oxidoreductase: The crystal structure of Ag(I) metallated azurin at 1.7 Å

Abstract

Bibliographical note

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