Molybdenum cofactor model systems

Stifel, E. L Coucouvanis, D. Newton, W. E., Eds. Molybdenum Enzymes, Cofactors and Model Systems, ACS Symposium Series 535 American Chemical Society Washington, DC, 1993 Chapters 10-23. 

Molybdenum is essential to the formation and activity of assimila-tory nitrate reductases. Cells must assimilate molybdate from the environment, metabolize molybdenum in some manner to form active molybdenum cofactor, and then incorporate it into a large molecular weight protein so that it can perform a reversible redox reaction with nitrate. Investigations on the aqueous Mo (III) model systems for nitrate reduction and the coordination of molybdate by naturally produced phenolates will hopefully lead to an understanding of the complex process of molybdenum acquisitions by and molybdenum function in nitrate reductases. 

Bolen, J.T., Cambasso, N., Muchmore, S.W., Morgan, T.V., and Mortenson, L. E. (1993) Structure and Environment of metal clusters of the nitrogenase molybdenum iron protein from Clostridium pasterianum, in Stiefel, E.I., Coucouvanis, D., and ewton, W.E. (eds.), Molibdenum Enzymes, Cofactors, and Model Systems, Am. Chem. Soc., Wahington, DC. 

W. E. Newton and D. R. Dean, Role of the iron-molybdenum cofactor polypeptide environment in azotobacter vinelandii-nitrogenase catalysis, in Molybdenum Enzymes, Cofactors and Model Systems , eds. E. I. Stiefel, D. Coucouvanis, and... 

T. Bolin, N. Campobasso, S. W. Muchmore, T. V. Morgan and L. E. Mortenson, Molybdenum Enzymes, Cofactors, and Model Systems, American Chemical Society, Washington, DC, 1993, p. 186. 

Bolin JT, Campobasso N, Muchmoee SW, Morgan TV and Moetenson LE (1993) The structure and environment of the metal clusters in the nitrogenase MoFe protein from Clostridium pasteurianum. In Stiefel El, Coucouvanis D and Newton WE, eds. Molybdenum enzymes, cofactors and model systems, pp. 186-195. American Chemical Society, Washington, D. C. 

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