Structural basis of interprotein electron transfer in bacterial sulfite oxidation

摘要

A key feature of many important chemical reactions in cells is the transfer of particles called electrons from one molecule to another. The sulfite oxidizing enzymes (or SOEs) are a group of enzymes that are found in many organisms. These enzymes convert sulfite, which is a very reactive compound that can damage cells, into another compound called sulfate. As part of this process the SOE transfers electrons from sulfite to other molecules, such as oxygen or a protein called cytochrome c. In the past, researchers have described the three-dimensional structure of three SOEs using a technique called X-ray crystallography. However, it has been difficult to study how SOEs pass electrons to other molecules because of the temporary nature of the interactions. McGrath et al. studied an SOE called SorT, which is found in bacteria. The SorT enzyme passes electrons from sulfite to another protein called SorU. McGrath used X-ray crystallography to determine the three-dimensional structures of versions of these proteins from a bacterium called Sinorhizobium meliloti. This included structures of the proteins on their own, and when they were bound to each other. These structures revealed that a subtle change in the shape of SorU occurs when the proteins interact, which enables an electron to be quickly transferred. McGrath et al. also found that the interface between the two proteins showed an unexpectedly high number of contact sites. These strengthen the interaction between the two proteins, which helps to make electron transfer more efficient. However, these contact sites do not prevent the two proteins from quickly moving apart after the electrons have been transferred. The next challenge is to find out whether these observations are common to SOEs from other forms of life.