NUCLEOTIDE IRON-SULFUR CLUSTER SIGNAL TRANSDUCTION IN THE NITROGENASE IRON-PROTEIN - THE ROLE OF ASP(125)

被引:76
作者
WOLLE, D [1 ]
DEAN, DR [1 ]
HOWARD, JB [1 ]
机构
[1] VIRGINIA POLYTECH INST & STATE UNIV,DEPT ANAEROB MICROBIOL,BLACKSBURG,VA 24061
关键词
D O I
10.1126/science.1359643
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Electron transfer in nitrogenase involves a gating process initiated by MgATP (magnesium adenosine triphosphate) binding to Fe-protein. The redox site, an 4Fe:4S cluster, is structurally separated from the MgATP binding site. For MgATP hydrolysis to be coupled to electron transfer, a signal transduction mechanism is proposed that is similar to that in guanosine triphosphatase proteins. Based on the three-dimensional structure of Fe-protein, Asp125 is likely to be part of a putative transduction path. Altered Fe-protein with Glu replacing Asp has been prepared and retains the ability for the initial nucleotide-dependent conformational change. However, either MgADP or MgATP can induce the shift and Mg binding to the nucleotide is no longer essential.
引用
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页码:992 / 995
页数:4
相关论文
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