VTVH-MCD Study of the ΔnifBΔnifZ MoFe Protein from Azotobacter vinelandii

被引：23

作者：

Cotton, Marcia S. ^{[2
]}

Rupnik, Kresimir ^{[2
]}

Broach, Robyn B. ^{[2
]}

Hu, Yilin ^{[1
]}

Fay, Aaron W. ^{[1
]}

Ribbe, Markus W. ^{[1
]}

Hales, Brian J. ^{[2
]}

机构：

[1] Univ Calif Irvine, Dept Mol Biol & Biochem, Irvine, CA 92697 USA

[2] Louisiana State Univ, Dept Chem, Baton Rouge, LA 70803 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2009年 / 131卷 / 13期

关键词：

COFACTOR;

D O I：

10.1021/ja807525m

中图分类号：

O6 [化学];

学科分类号：

070301 [无机化学];

摘要：

NifZ is a member of a series of proteins associated with the maturation of the nitrogenase MoFe protein. An MCD spectroscopic study was undertaken on the Delta nifB Delta nifZ MoFe protein generated in the absence of both NifZ and NifB (deletion of NifB generates an apo-MoFe protein tacking the FeMo cofactor). Results presented here show that, in the absence of NifZ, only one of the two P-clusters of the MoFe protein is matured to the ultimate [8Fe-7S] structure. The other P-cluster site in the protein contains a [4Fe-4S] cluster pair, representing a P-cluster precursor that is electronically identical to the analogous clusters observed in the Delta nifH MoFe protein. These results suggest that the MoFe protein is synthesized in a stepwise fashion where NifZ is specifically required for the formation of the second P-cluster.

引用

页码：4558 / +

页数：3

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