Nitrogenase fixation

Many key protein ET processes have become accessible to theoretical analysis recently because of high-resolution x-ray stmctural data. These proteins include the bacterial photosynthetic reaction centre [18], nitrogenase (responsible for nitrogen fixation), and cytochrome c oxidase (the tenninal ET protein in mammals) [19, 20]. Although much is understood about ET in these molecular machines, considerable debate persists about details of the molecular transfonnations. 

Free-living bacteria are, however, used as the source of the enzyme nitrogenase, responsible for N2 fixation (1,4,26,80), for research purposes because these ate easier to culture. The enzyme is virtually identical to that from the agriculturally important thizobia. These free-living N2-fixets can be simply classified into aerobes, anaerobes, facultative anaerobes, photosynthetic bacteria, and cyanobacteria. 

Non-enzvmatic simulation of nitrogenase reactions and the mechanism of biological nitrogen fixation. G. N. Schrauzer, Angew. Chem., Int. Ed. Engl., 1975, 14, 514-522 (36). 

The chemistry of nitrogen fixation and models of the reactions of nitrogenase. R. A. Henderson,... 

Not surprisingly, only about 20 of the chemical elements found on Earth are used by living organisms (Chapters 3 and 8). Most of them are common elements. Rare elements are used, if at all, only at extremely low concentrations for specialized functions. An example of the latter is the use of molybdenum as an essential component of nitrogenase, the enzyme that catalyzes the fixation of elemental dinitrogen. Because they are composed of common elements, living organisms exert their most profound effects on the cycles of those elements. 

Fig. 12. The nitrogen fixation genes of Azotobacter vinelandii. This orgEinism has three nitrogenase systems, viz nif, vnf, and anf, which it uses for fixing N2 under different environmental conditions. The boxes with slanted hatching indicate the structural genes of the three systems, those colored dark gray are required for eiU three systems, and those with vertical hatching are required for both the vnf and anf systems.

The elucidation of the crystal structures of two high-spin EPR proteins has shown that the proposals for novel Fe-S clusters are not without substance. Two, rather than one novel Fe-S cluster, were shown to be present in nitrogenase, the key enzyme in the biotic fixation of molecular nitrogen 4, 5). Thus the FeMoco-cofactor comprises two metal clusters of composition [4Fe-3S] and [lMo-3Fe-3S] bridged by three inorganic sulfur atoms, and this is some 14 A distant from the P-cluster, which is essentially two [4Fe-4S] cubane moieties sharing a corner. The elucidation of the crystal structure of the Fepr protein (6) provides the second example of a high-spin EPR protein that contains yet another unprecedented Fe-S cluster. 

In nature, nitrogen fixation is accomplished by nitrogenase, an enzyme that binds N2 and weakens its bonding sufficiently to break the triple bond. Only a few algae and bacteria contain nitrogenase. Our Chemishy and Life Box describes what is known about this enzyme. 

Yoch DC (1979) Manganese, an essential trace element for N2 fixation by Rhodospirilllum rubrum and Rhodopseudomonas capsulata role in nitrogenase regulation 7 BacterioZ 140 987-995. 

Iron-sulfur (Fe-S) proteins function as electron-transfer proteins in many living cells. They are involved in photosynthesis, cell respiration, as well as in nitrogen fixation. Most Fe-S proteins have single-iron (rubredoxins), or two-, three-, or four-iron (ferredoxins), or even seven/eight-iron (nitrogenases) centers. 

In Nature, nitrogen fixation is mediated by the enzyme nitrogenase according to Eq. (1) (6)... 

---