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Di-iron-carboxylate proteins

P Nordlund¹, H Eklund

¹University of Stockholm, Sweden.

Current Opinion in Structural Biology

|December 1, 1995

Summary

Di-iron proteins utilize carboxylate and oxide bridges for dioxygen chemistry. Their flexible dinuclear iron centers enable efficient oxygen activation in hydroxylase-oxidase enzymes.

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Area of Science:

Biochemistry
Structural Biology
Enzymology

Background:

Di-iron centers are crucial motifs in proteins catalyzing dioxygen chemistry and phosphoryl transfer.
These centers are typically bridged by carboxylate residues and oxide/hydroxide groups, coordinated by histidines and carboxylates.

Purpose of the Study:

To elucidate the structural and mechanistic basis of di-iron protein function in dioxygen chemistry.
To correlate structural flexibility with the catalytic efficiency of hydroxylase-oxidase enzymes.

Main Methods:

Analysis of recent structural data for di-iron enzymes.
Integration of spectroscopic and kinetic data.
Mechanistic interpretation based on integrated data.

Main Results:

Di-iron centers exhibit flexibility in coordinating carboxylate groups within hydroxylase-oxidase enzymes.
Low coordination numbers and buried active sites are characteristic of these enzymes.
These features facilitate the efficient utilization of molecular oxygen's oxidation potential.

Conclusions:

Structural flexibility of di-iron sites is key to the function of hydroxylase-oxidase enzymes like ribonucleotide reductase and methane monooxygenase.
The unique coordination environment enables efficient harnessing of molecular oxygen for oxidative catalysis.

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