English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Azurin as a Protein Scaffold for a Low-coordinate Nonheme Iron Site with a Small-molecule Binding Pocket

McLaughlin, M. P., Retegan, M., Bill, E., Payne, T. M., Shafaat, H. S., Peña, S., et al. (2012). Azurin as a Protein Scaffold for a Low-coordinate Nonheme Iron Site with a Small-molecule Binding Pocket. Journal of the American Chemical Society, 134(48), 19746-19757. doi:10.1021/ja308346b.

Item is

Basic

show hide
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
McLaughlin, Matthew P.1, Author
Retegan, Marius2, Author              
Bill, Eckhard2, Author              
Payne, Thomas M.3, Author
Shafaat, Hannah S.4, Author              
Peña, Salvador1, Author
Sudhamsu, Jawahar3, Author
Ensign, Amy A.1, Author
Crane, Brian R.3, Author
Neese, Frank2, Author              
Holland, Patrick L.1, Author
Affiliations:
1Department of Chemistry, University of Rochester, Rochester, New York 14618, United States, ou_persistent22              
2Research Department Neese, Max Planck Institute for Chemical Energy Conversion, Max Planck Society, ou_3023886              
3Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, United States, ou_persistent22              
4Research Department Lubitz, Max Planck Institute for Chemical Energy Conversion, Max Planck Society, ou_3023873              

Content

show
hide
Free keywords: -
 Abstract: The apoprotein of Pseudomonas aeruginosa azurin binds iron(II) to give a 1:1 complex, which has been characterized by electronic absorption, Mössbauer, and NMR spectroscopies, as well as X-ray crystallography and quantum-chemical computations. Despite potential competition by water and other coordinating residues, iron(II) binds tightly to the low-coordinate site. The iron(II) complex does not react with chemical redox agents to undergo oxidation or reduction. Spectroscopically calibrated quantum-chemical computations show that the complex has high-spin iron(II) in a pseudotetrahedral coordination environment, which features interactions with side chains of two histidines and a cysteine as well as the C═O of Gly45. In the 5A1 ground state, the dz2 orbital is doubly occupied. Mutation of Met121 to Ala leaves the metal site in a similar environment but creates a pocket for reversible binding of small anions to the iron(II) center. Specifically, azide forms a high-spin iron(II) complex and cyanide forms a low-spin iron(II) complex.

Details

show
hide
Language(s): eng - English
 Dates: 2012-08-222012-11-202012-12-05
 Publication Status: Published in print
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/ja308346b
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of the American Chemical Society
  Other : JACS
  Abbreviation : J. Am. Chem. Soc.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Washington, DC : American Chemical Society
Pages: - Volume / Issue: 134 (48) Sequence Number: - Start / End Page: 19746 - 19757 Identifier: ISSN: 0002-7863
CoNE: https://pure.mpg.de/cone/journals/resource/954925376870