期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 134, 期 48, 页码 19746-19757出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja308346b
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资金
- National Institutes of Health [GM-065313, TM-GM-008267]
- Fulbright Foundation
- Alexander von Humboldt Foundation
- Max-Planck-Gesellschaft
- National Science Foundation [CHE-0749997]
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [0749997] Funding Source: National Science Foundation
The apoprotein of Pseudomonas aeruginosa azurin binds iron(II) to give a 1:1 complex, which has been characterized by electronic absorption, Mossbauer, 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 (5)A(1) ground state, the d(z2) 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.
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