Nitrogen Nitrogenase

In the absence of molecular nitrogen, nitrogenase produces molecular hydrogen. This hydrogenase reaction (EC 1.18.99.1) is represented by the following chemical reaction ... 

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. 

The nitrogenase system reduces hundreds of millions of kilograms of nitrogen gas to ammonia each year, catalysing tire reaction at ambient temperatures and atmospheric pressure. Nitrogenase consists of two proteins tliat contain... 

A number of nitrogen-fixing bacteria contain vanadium and it has been shown that in one of these, Azotobacter, there are three distinct nitrogenase systems based in turn on Mo, V and Fe, each of which has an underlying functional and structural similarity.This discovery has prompted a search for models and the brown compound [Na(thf)]+[V(N2)2(dppe)2] (dppe = Pli2PCH2CH2PPh2) has recently been prepared by reduction of VCI3 by sodium naphthalenide... 

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,... 

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. 

Fallik E, Y-K Chan, RL Robson (1991) Detection of alternative nitrogenases in aerobic gram-negative nitrogen-fixing bacteria. J Bacteriol 173 365-371. 

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. 

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