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If oxygen becomes the undoing of proteins
Date:10/12/2011

red by the BMBF, it was possible to show the diverse phases of the inactivation process for the first time using the so-called X-ray absorption spectroscopy. The researchers used the synchroton radiation source Swiss Light Source in Switzerland for this specific type of measurement. It generates particularly strong rays, thus enabling the characterization of metal centers in proteins. Amongst other things, the scientists thus determined the chemical nature of the iron centers and the distance from the surrounding atoms using atomic resolution.

Inactivation in three phases

The team of researchers from Bochum and Berlin used a new experimental procedure. They initially brought the hydrogenase sample into contact with oxygen for a few seconds to minutes and finally for a couple of hours and then suppressed all proceeding reactions by deep-freezing it in liquid nitrogen. The subsequently gained spectroscopic data was used for the development of a model for a three-phase inactivation process. According to this model, an oxygen molecule initially binds to the di-iron center of the hydrogenase, which leads to the development of an aggressive oxygen species. In the subsequent phase, this attacks and modifies the four-iron center. During the final phase, further oxygen molecules bind and the entire complex disintegrates. "The entire process thus consists of a number of consecutive reactions that are distinctly separated in time", says Lambertz. "The velocity of the entire process is possibly dependent on the phase during which the aggressive oxygen species moves from the di-iron to the four-iron center. We are currently elaborating further experiments to investigate this."


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Contact: Camilla Lambertz
Camilla.Lambertz@rub.de
49-234-322-4496
Ruhr-University Bochum
Source:Eurekalert

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