3 research outputs found
Azurin as a Protein Scaffold for a Low-coordinate Nonheme Iron Site with a Small-molecule Binding Pocket
The apoprotein of <i>Pseudomonas aeruginosa</i> azurin
binds ironĀ(II) to give a 1:1 complex, which has been characterized
by electronic absorption, MoĢssbauer, and NMR spectroscopies,
as well as X-ray crystallography and quantum-chemical computations.
Despite potential competition by water and other coordinating residues,
ironĀ(II) binds tightly to the low-coordinate site. The ironĀ(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 ironĀ(II) in a pseudotetrahedral
coordination environment, which features interactions with side chains
of two histidines and a cysteine as well as the Cī»O of Gly45.
In the <sup>5</sup>A<sub>1</sub> ground state, the <i>d</i><sub><i>z</i><sup>2</sup></sub> 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
ironĀ(II) center. Specifically, azide forms a high-spin ironĀ(II) complex
and cyanide forms a low-spin ironĀ(II) complex
Azurin as a Protein Scaffold for a Low-coordinate Nonheme Iron Site with a Small-molecule Binding Pocket
The apoprotein of <i>Pseudomonas aeruginosa</i> azurin
binds ironĀ(II) to give a 1:1 complex, which has been characterized
by electronic absorption, MoĢssbauer, and NMR spectroscopies,
as well as X-ray crystallography and quantum-chemical computations.
Despite potential competition by water and other coordinating residues,
ironĀ(II) binds tightly to the low-coordinate site. The ironĀ(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 ironĀ(II) in a pseudotetrahedral
coordination environment, which features interactions with side chains
of two histidines and a cysteine as well as the Cī»O of Gly45.
In the <sup>5</sup>A<sub>1</sub> ground state, the <i>d</i><sub><i>z</i><sup>2</sup></sub> 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
ironĀ(II) center. Specifically, azide forms a high-spin ironĀ(II) complex
and cyanide forms a low-spin ironĀ(II) complex
Azurin as a Protein Scaffold for a Low-coordinate Nonheme Iron Site with a Small-molecule Binding Pocket
The apoprotein of <i>Pseudomonas aeruginosa</i> azurin
binds ironĀ(II) to give a 1:1 complex, which has been characterized
by electronic absorption, MoĢssbauer, and NMR spectroscopies,
as well as X-ray crystallography and quantum-chemical computations.
Despite potential competition by water and other coordinating residues,
ironĀ(II) binds tightly to the low-coordinate site. The ironĀ(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 ironĀ(II) in a pseudotetrahedral
coordination environment, which features interactions with side chains
of two histidines and a cysteine as well as the Cī»O of Gly45.
In the <sup>5</sup>A<sub>1</sub> ground state, the <i>d</i><sub><i>z</i><sup>2</sup></sub> 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
ironĀ(II) center. Specifically, azide forms a high-spin ironĀ(II) complex
and cyanide forms a low-spin ironĀ(II) complex