English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

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

MPS-Authors
/persons/resource/persons237685

Retegan,  Marius
Research Department Neese, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

/persons/resource/persons137604

Bill,  Eckhard
Research Department Neese, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

/persons/resource/persons237716

Shafaat,  Hannah S.
Research Department Lubitz, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

/persons/resource/persons216825

Neese,  Frank
Research Department Neese, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

External Ressource
No external resources are shared
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

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.


Cite as: http://hdl.handle.net/21.11116/0000-0007-E5AA-7
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.