Structural basis of biological nitrogen fixation

Article Abstract:

The biological nitrogen fixation enzyme, nitrogenase, consists of two-component metalloproteins comprising of the iron (Fe) protein and the molybdenum iron (MoFe) protein. The reduction of the substrate by nitrogenase involves the reduction of Fe protein by ferredoxins and flavodoxins, transfer of single electron from Fe protein to MoFe protein, and an electron transfer to the active site within the MoFe protein. The Fe proteins have 4Fe-4S clusters and MoFe proteins contains the active site. A P-cluster transfers electrons between the 4Fe-4S cluster and the FeMo cofactor

Nitrogenase, Nitrogen, Nitrogen fixation

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Transferrin as a metal ion mediator

Article Abstract:

Transferrin is a naturally occurring protein that could be used to ensure that metal-based drugs or diagnostic agents reach their target. Transferrin binds two iron molecules, transfers them into cells, and then releases the iron. Transferrin can bind to other metal ions and the transferrin receptor will still recognize the metal-protein complex.

Transferrin, Biological transport, Active, Active biological transport

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Nucleic acid recognition by metal complexes of bleomycin

Article Abstract:

Research on the metallobleomycins may lead to analogues of the drug that are more effective in treating cancer. Bleomycin is a natural product that breaks DNA but it requires metal ions and oxygen in order to do this. The structure of several metallobleomycins is disussed.

Bleomycin

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