CJCU

Chem. J. Chinese Universities ›› 2000, Vol. 21 ›› Issue (S1): 152.

• Chemistry in Life Sciences • Previous Articles     Next Articles

The Effects of Citrato Molybdate on the Growth, Rate of Azotobacter Vinelandii

QIU Xue-Hui1, DONG En-Heng1, ZHOU Zhao-Hui2, LONG Ming-Nan1, ZHANG Feng-Zhang1, XU Liang-Shu1, WAN Hui-Lin2   

  1. 1. Department of Biology, Xiamen University, Xiamen 361005;
    2. Department of Chemistry, Xiamen University, Xiamen 361005
  • Online:2000-12-31 Published:2000-12-31
  • Supported by:

    Financial supports from the National Natural Science Foundation of China (Grant Nos. 39970176 and 29933040) are gratefully acknowledged.

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Abstract:

An iron-molybdenum cofactor (FeMoco or M-cluster) of nitrogenase is believed to be the active center for the N2-binding and reduction. Recent X-ray crystal structure of MoFe-protein revealed the FeMoco as FeS3Fe3(S)3Fe3S3Mo(R-homocitrate) cluster and the biosynthesis of FeMoco requires at least six nif gene products. FeMoco should be assembled firstly and then inserted into the FeMoco-deficient dinitrogenase. It has been known that the NifB-co, the product of nifB, is an iron and sulfur-containing precursor of FeMoco. However, how the molybdenum and homocitrate are assembled into molybdenum free NifB-co remains unknown.

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