高等学校化学学报 ›› 2000, Vol. 21 ›› Issue (S1): 152.
• Chemistry in Life Sciences • 上一篇 下一篇
QIU Xue-Hui1, DONG En-Heng1, ZHOU Zhao-Hui2, LONG Ming-Nan1, ZHANG Feng-Zhang1, XU Liang-Shu1, WAN Hui-Lin2
QIU Xue-Hui1, DONG En-Heng1, ZHOU Zhao-Hui2, LONG Ming-Nan1, ZHANG Feng-Zhang1, XU Liang-Shu1, WAN Hui-Lin2
摘要:
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.
TrendMD: