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Milestone In Mitochondrial Structure Revealed

ebilitate the normal operations of cells which, in turn, poses mounting problems for tissues and organs. Impeded electron flow also promotes the production of oxygen free-radical molecules which can attack all components of a cell and cause mutations in both nuclear and mitochondrial DNA.

As determined by Jap and his colleagues, the structure of cytochrome bc1 is that of a dimer, a complex of two neighboring molecular chains called monomers. The shape of the dimer is considered essential to its role in the electron-transfer process which is carried out in a hollow between its two monomers. This work has provided structural confirmation of the hollow's existence.

The cytochrome bc1 dimer is a non-crystalline protein embedded in the lipids of the mitochondrial inner membrane. Coaxing the protein into forming a crystal, a pre-requisite for x-ray imaging, was a major challenge.

"To crystallize cytochrome bc1 we had to first purify the protein by breaking the membrane using just the right proportion of a specific detergent," says Jap. "It is one of the most difficult of all crystallization techniques to carry out, but we now have one of the finest collections of (cytochrome bc1) crystals known. Without these high-quality crystals, we could not have achieved success."

With the solving of the cytochrome bc1 structure, scientists now have more than half of the mitochondrial respiratory chain filled in. What remains is the small complex II protein, and the very large complex I protein. Jap and his group will join the effort underway to solve complex I. For this, he plans to try a new strategy, one in which he will combine x-ray and electron crystallography techniques. This approach will include the use of multiple crystal averaging and phase information from both heavy atom derivatives and electron micrographs. Despite the small size of the complex II protein, its structure will also have to be solved.

As Jap explains, "Scientists need to have the resources
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Contact: Lynn Yarris
lcyarris@lbl.gov
(510) 486-5375
DOE/Lawrence Berkeley National Laboratory
18-Aug-1998


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