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image of Israel Journal of Plant Sciences

The requirements for ATP and reductant during diazotrophic growth, the physicochemical properties of the nitrogenase proteins, and the involvement of Mo in different aspects of N2 fixation are reviewed. Irrespective of the source from which it is isolated, nitrogenase has very similar properties and is comprised of two O2-sensitive redox proteins. The Mo—Fe protein is an α2β2 tetramer of MW 220000, containing 2 Mo and approx. 33 ± 3 Fe and acid-labile S atoms per tetramer. The Mo atoms and approx. 40% of the Fe atoms can be extracted with N-methylformamide as a unique cofactor (FeMoco) which contains Mo, Fe and S2- in the ratios 1:8:4. Cluster extrusion and Mössbauer data are consistent with the presence of four 4Fe4S clusters in addition to two FeMoco clusters. The binding of substrate (C2H2), its reduction product C2H4, and the inhibitor CO to the Mo-Fe protein have been investigated by EPR spectroscopy. The Fe protein is γ2 dimer of MW 67000; spectroscopic and extrusion data indicate the presence of a single 4Fe4S cluster. Both proteins bind MgATP but only the Mo—Fe protein catalyses the exchange of 32PO2- 4 into both ADP and ATP. Mo is involved in regulating expression of the nitrogen fixation (nif) genes in a number of organisms. In Klebsiella pneumoniae, nif-lac gene fusions have shown that maximum expression from the nifH promoter only occurs in the presence of Mo. Data are presented showing that nif-lac fusions of nifK and nifD behave similarly, i.e. Mo is required for maximum expression of all the structural genes of nitrogenase. The uptake, storage and processing of Mo in N2-fixing organisms is discussed.

Affiliations: 1: Agricultural Research Council, Unit of Nitrogen Fixation, University of Sussex


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