Transforming a Blue Copper into a Red Copper Protein: Engineering Cysteine and Homocysteine into the Axial Position of Azurin Using Site-Directed Mutagenesis and Expressed Protein Ligation-Reference-Cited by-同舟云学术

Transforming a Blue Copper into a Red Copper Protein: Engineering Cysteine and Homocysteine into the Axial Position of Azurin Using Site-Directed Mutagenesis and Expressed Protein Ligation

Published:2010-07-07 Issue:29 Volume:132 Page:10093-10101
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Clark Kevin M.¹,Yu Yang¹,Marshall Nicholas M.¹,Sieracki Nathan A.¹,Nilges Mark J.¹,Blackburn Ninian J.¹,van der Donk Wilfred A.¹,Lu Yi¹

Affiliation:

1. Department of Biochemistry, Center of Biophysics and Computational Biology, Department of Chemistry, Illinois EPR Research Center, University of Illinois at Urbana−Champaign, 600 South Mathews Avenue, Urbana, Illinois 61801, and Department of Science and Engineering, Oregon Health and Science University, Beaverton, Oregon 97006

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja102632p

Reference72 articles.

1. Rack-induced bonding in blue-copper proteins

2. Theoretical Study of the Electronic Spectrum of Plastocyanin

3. Electronic structures of active sites in copper proteins: contributions to reactivity

4. Resonance Raman spectroscopy of the azurin His117Gly mutant. Interconversion of type 1 and type 2 copper sites through exogenous ligands

5. Resonance Raman excitation profiles indicate multiple Cys .fwdarw. Cu charge transfer transitions in type 1 copper proteins

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