Distance between atoms is key to iron protein function

ANN ARBOR---Geometry is destiny in the molecular world where small structural changes can mean big functional differences. According to University of Michigan chemist James Penner-Hahn, this is especially true for non-heme diiron proteins that use iron and oxygen to regulate important biological functions.

In a paper published in the Jan. 7 issue of Science, Penner-Hahn and colleagues describe how they used analytical techniques to probe the molecular structure of peroxide intermediates in diiron proteins. While scientists have known for years that diiron proteins carry out a variety of biological functions, recent work has shown that many of these proteins pass through a peroxide-bridged intermediate state as part of their reaction with oxygen.

Sometimes the peroxide-bridged intermediate works as part of an enzyme to activate oxygen for critical reactions, such as synthesizing DNA building blocks or converting methane into methanol. Sometimes, in a process called biomineralization, the same intermediate is used to store iron atoms within the protective protein envelope of the iron-storage protein, ferritin.

"The puzzle has been how the same intermediate can act as a catalyst with oxygen-activating enzymes, but act as a substrate with ferritin proteins," said Penner-Hahn, a U-M professor of chemistry.

The answer appears to be an unusually short distance of 2.53 angstroms between iron atoms in the peroxide-bridged ferritin intermediate---a distance about 0.5 to 1.5 angstroms shorter than that between iron atoms in other peroxide-bridged intermediates.

"Half an angstrom is miniscule compared to the size of a protein, but it's the equivalent of the Grand Canyon on an atomic scale," Penner-Hahn explained. "The shorter distance between iron atoms forces the ferritin diiron site into an unusual geometry that should strengthen the O-O bond [the bond between oxygen atoms] and thus favo

Contact: James Penner-Hahn or Sally Pobojewski
University of Michigan

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