Spectroscopic Characterization of the Isolated Iron-Molybdenum Cofactor (FeMoco) Precursor from the Protein NifEN

被引：46
作者：
Fay, Aaron W. [1 ]
Blank, Michael A. [2 ]
Lee, Chi Chung [1 ]
Hu, Yilin [1 ]
Hodgson, Keith O. [2 ,3 ]
Hedman, Britt [3 ]
Ribbe, Markus W. [1 ]
机构：
[1] Univ Calif Irvine, Dept Mol Biol & Biochem, Irvine, CA 92697 USA
[2] Stanford Univ, Dept Chem, Stanford, CA 94305 USA
[3] Stanford Univ, SLAC, Stanford Synchrotron Radiat Lightsource, Menlo Pk, CA 94025 USA
来源：
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2011年 / 50卷 / 34期
关键词：
biosynthesis; FeMoco; nitrogenase; precursors; XAS/EXAFS; NITROGENASE MOFE-PROTEIN; MECHANISM;
D O I：
10.1002/anie.201102724
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
The fate of iron eight: The active site of Mo-nitrogenase is FeMoco. Previously, a FeMoco precursor was captured on NifEN, a scaffold protein for FeMoco biosynthesis. The FeMoco precursor is now isolated from the NifEN. The integrity of the precursor is shown by its full catalytic activity on incorporation into precursor-deficient NifEN. XAS/EXAFS analysis supports the eight-iron model of the precursor (see structure: Fe purple, S yellow). © 2011 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
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收藏
页码：7787 / 7790
页数：4
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