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Title: A purple cupredoxin from Nitrosopumilus maritimus containing a mononuclear type 1 copper center with an open binding site

Mononuclear cupredoxin proteins usually contain a coordinately saturated type 1 copper (T1Cu) center and function exclusively as electron carriers. Here we report a cupredoxin isolated from the nitrifying archaeon Nitrosopumilus maritimus SCM1, called Nmar1307, that contains a T1Cu center with an open binding site containing water. It displays a deep purple color due to strong absorptions around 413 nm (1880 M –1 cm –1) and 558 nm (2290 M –1 cm –1) in the UV–vis electronic spectrum. EPR studies suggest the protein contains two Cu(II) species of nearly equal population, one nearly axial, with hyperfine constant A = 98 × 10 –4 cm –1, and another more rhombic, with a smaller A value of 69 × 10 –4 cm –1. The X-ray crystal structure at 1.6 Å resolution confirms that it contains a Cu atom coordinated by two His and one Cys in a trigonal plane, with an axial H 2O at 2.25 Å. Both UV–vis absorption and EPR spectroscopic studies suggest that the Nmar1307 can oxidize NO to nitrite, an activity that is attributable to the high reduction potential (354 mV vs SHE) of the copper site. Lastly, these results suggest that mononuclear cupredoxins can have amore » wide range of structural features, including an open binding site containing water, making this class of proteins even more versatile.« less
Authors:
 [1] ;  [1] ;  [1] ;  [1] ;  [1] ;  [1] ;  [1] ;  [2] ;  [3] ;  [1] ;  [1]
  1. Univ. of Illinois at Urbana-Champaign, Urbana, IL (United States)
  2. Brookhaven National Lab. (BNL), Upton, NY (United States)
  3. Univ. of Washington, Seattle, WA (United States)
Publication Date:
Report Number(s):
BNL-112067-2016-JA
Journal ID: ISSN 0002-7863
Grant/Contract Number:
SC00112704
Type:
Accepted Manuscript
Journal Name:
Journal of the American Chemical Society
Additional Journal Information:
Journal Volume: 138; Journal Issue: 20; Journal ID: ISSN 0002-7863
Publisher:
American Chemical Society (ACS)
Research Org:
Brookhaven National Laboratory (BNL), Upton, NY (United States)
Sponsoring Org:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE
OSTI Identifier:
1340348

Hosseinzadeh, Parisa, Tian, Shiliang, Marshall, Nicholas M., Hemp, James, Mullen, Timothy, Nilges, Mark J., Gao, Yi -Gui, Robinson, Howard, Stahl, David A., Gennis, Robert B., and Lu, Yi. A purple cupredoxin from Nitrosopumilus maritimus containing a mononuclear type 1 copper center with an open binding site. United States: N. p., Web. doi:10.1021/jacs.5b13128.
Hosseinzadeh, Parisa, Tian, Shiliang, Marshall, Nicholas M., Hemp, James, Mullen, Timothy, Nilges, Mark J., Gao, Yi -Gui, Robinson, Howard, Stahl, David A., Gennis, Robert B., & Lu, Yi. A purple cupredoxin from Nitrosopumilus maritimus containing a mononuclear type 1 copper center with an open binding site. United States. doi:10.1021/jacs.5b13128.
Hosseinzadeh, Parisa, Tian, Shiliang, Marshall, Nicholas M., Hemp, James, Mullen, Timothy, Nilges, Mark J., Gao, Yi -Gui, Robinson, Howard, Stahl, David A., Gennis, Robert B., and Lu, Yi. 2016. "A purple cupredoxin from Nitrosopumilus maritimus containing a mononuclear type 1 copper center with an open binding site". United States. doi:10.1021/jacs.5b13128. https://www.osti.gov/servlets/purl/1340348.
@article{osti_1340348,
title = {A purple cupredoxin from Nitrosopumilus maritimus containing a mononuclear type 1 copper center with an open binding site},
author = {Hosseinzadeh, Parisa and Tian, Shiliang and Marshall, Nicholas M. and Hemp, James and Mullen, Timothy and Nilges, Mark J. and Gao, Yi -Gui and Robinson, Howard and Stahl, David A. and Gennis, Robert B. and Lu, Yi},
abstractNote = {Mononuclear cupredoxin proteins usually contain a coordinately saturated type 1 copper (T1Cu) center and function exclusively as electron carriers. Here we report a cupredoxin isolated from the nitrifying archaeon Nitrosopumilus maritimus SCM1, called Nmar1307, that contains a T1Cu center with an open binding site containing water. It displays a deep purple color due to strong absorptions around 413 nm (1880 M–1 cm–1) and 558 nm (2290 M–1 cm–1) in the UV–vis electronic spectrum. EPR studies suggest the protein contains two Cu(II) species of nearly equal population, one nearly axial, with hyperfine constant A∥ = 98 × 10–4 cm–1, and another more rhombic, with a smaller A∥ value of 69 × 10–4 cm–1. The X-ray crystal structure at 1.6 Å resolution confirms that it contains a Cu atom coordinated by two His and one Cys in a trigonal plane, with an axial H2O at 2.25 Å. Both UV–vis absorption and EPR spectroscopic studies suggest that the Nmar1307 can oxidize NO to nitrite, an activity that is attributable to the high reduction potential (354 mV vs SHE) of the copper site. Lastly, these results suggest that mononuclear cupredoxins can have a wide range of structural features, including an open binding site containing water, making this class of proteins even more versatile.},
doi = {10.1021/jacs.5b13128},
journal = {Journal of the American Chemical Society},
number = 20,
volume = 138,
place = {United States},
year = {2016},
month = {4}
}