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  Outer-Sphere Contributions to the Electronic Structure of Type Zero Copper Proteins

Lancester, K. M., Zaballa, M.-E., Sproules, S., Sundararajan, M., DeBeer, S., Richards, J. H., et al. (2012). Outer-Sphere Contributions to the Electronic Structure of Type Zero Copper Proteins. Journal of the American Chemical Society, 134(19), 8241-8253. doi:10.1021/ja302190r.

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 Creators:
Lancester, Kyle M.1, 2, Author
Zaballa, María-Eugenia3, Author
Sproules, Stephen4, Author
Sundararajan, Mahesh5, 6, Author
DeBeer, Serena2, 7, Author              
Richards, John H.1, Author
Vila, Alejandro J.3, Author
Neese, Frank5, 7, Author              
Gray, Harry B.1, Author
Affiliations:
1Beckman Institute, California Institute of Technology, Pasadena, California 91125, United States, ou_persistent22              
2Department of Chemistry and Chemical Biology, Cornell University, Baker Laboratory, Ithaca, New York 14853, United States, ou_persistent22              
3Instituto de Biología Molecular y Celular de Rosario, (IBR-CONICET), Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Suipacha 531 (S2002LRK), Rosario, Argentina, ou_persistent22              
4EPSRC National UK EPR Facility and Service, Photon Science Institute, The University of Manchester, Oxford Road, Manchester M13 9PL, U.K., ou_persistent22              
5Institute for Physical and Theoretical Chemistry, University of Bonn, Wegelerstrasse 12, Bonn-53115, Germany, ou_persistent22              
6Theoretical Chemistry Section, Chemistry Group, Bhabha Atomic Research Centre, Mumbai-400 085, India, ou_persistent22              
7Research Department Neese, Max Planck Institute for Bioinorganic Chemistry, Max Planck Society, ou_3023879              

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 Abstract: Bioinorganic canon states that active-site thiolate coordination promotes rapid electron transfer (ET) to and from type 1 copper proteins. In recent work, we have found that copper ET sites in proteins also can be constructed without thiolate ligation (called “type zero” sites). Here we report multifrequency electron paramagnetic resonance (EPR), magnetic circular dichroism (MCD), and nuclear magnetic resonance (NMR) spectroscopic data together with density functional theory (DFT) and spectroscopy-oriented configuration interaction (SORCI) calculations for type zero Pseudomonas aeruginosa azurin variants. Wild-type (type 1) and type zero copper centers experience virtually identical ligand fields. Moreover, O-donor covalency is enhanced in type zero centers relative that in the C112D (type 2) protein. At the same time, N-donor covalency is reduced in a similar fashion to type 1 centers. QM/MM and SORCI calculations show that the electronic structures of type zero and type 2 are intimately linked to the orientation and coordination mode of the carboxylate ligand, which in turn is influenced by outer-sphere hydrogen bonding.

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Language(s): eng - English
 Dates: 2012-03-132012-05-072012-05-16
 Publication Status: Published in print
 Pages: 13
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/ja302190r
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Title: Journal of the American Chemical Society
  Other : JACS
  Abbreviation : J. Am. Chem. Soc.
Source Genre: Journal
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Publ. Info: Washington, DC : American Chemical Society
Pages: - Volume / Issue: 134 (19) Sequence Number: - Start / End Page: 8241 - 8253 Identifier: ISSN: 0002-7863
CoNE: https://pure.mpg.de/cone/journals/resource/954925376870