Nitrogenase: Difference between revisions

Student (talk | contribs)
No edit summary
Student (talk | contribs)
No edit summary
Line 17: Line 17:
At the bottom of the protein, where the Fe protein comes into contact with the FeMo protein, is a <scene name='Sandbox_10/1n2c_fes_cluster_cys/1'>4Fe:4S cluster</scene>, held in place by cysteines. This cluster accepts electrons from ferredoxin and gives electrons to the FeMo protein.
At the bottom of the protein, where the Fe protein comes into contact with the FeMo protein, is a <scene name='Sandbox_10/1n2c_fes_cluster_cys/1'>4Fe:4S cluster</scene>, held in place by cysteines. This cluster accepts electrons from ferredoxin and gives electrons to the FeMo protein.


When the Fe protein is bound to the FeMo protein <scene name='Sandbox_10/1n2c_single_complex/2'>(zoom out)</scene>, ATP is hydrolyzed and electrons that were transferred to the 4Fe:4S cluster of the Fe protein by ferredoxin are transferred to the FeMo protein. The crystal structure of the complete nitrogenase complex reveals how the binding of the Fe and FeMo proteins, the hydrolysis of ATP, and the transfer of electrons are all coupled.  
When the Fe protein is bound to the FeMo protein (<scene name='Sandbox_10/1n2c_single_complex/2'>zoom out</scene>), ATP is hydrolyzed and electrons that were transferred to the 4Fe:4S cluster of the Fe protein by ferredoxin are transferred to the FeMo protein. The crystal structure of the complete nitrogenase complex reveals how the binding of the Fe and FeMo proteins, the hydrolysis of ATP, and the transfer of electrons are all coupled.  


Compared to the crystal structure of Fe protein that is not bound to FeMo protein, Fe protein complexed with FeMo protein  
Compared to the crystal structure of Fe protein that is not bound to FeMo protein, Fe protein complexed with FeMo protein  

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Student, Eran Hodis, David Canner, Michal Harel, Alexander Berchansky, Joel L. Sussman