The interstitial atom of the nitrogenase FeMo-Cofactor: ENDOR and ESEEM evidence that it is not a nitrogen

被引：61

作者：

Yang, TC

Maeser, NK

Laryukhin, M

Lee, HI

Dean, DR ^{[1
]}

Seefeldt, LC

Hoffman, BM

机构：

[1] Virginia Polytech Inst & State Univ, Dept Biochem, Blacksburg, VA 24061 USA

[2] Northwestern Univ, Dept Chem, Evanston, IL 60208 USA

[3] Utah State Univ, Dept Chem & Biochem, Logan, UT 84322 USA

[4] Kyungpook Natl Univ, Dept Chem Educ, Taegu 702701, South Korea

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2005年 / 127卷 / 37期

关键词：

D O I：

10.1021/ja0552489

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

X-ray crystallographic study of the nitrogenase MoFe protein revealed electron density from an atom (denoted X) inside the active-site metal cluster, the [MoFe7S9:homocitrate] FeMo-cofactor. The electron density associated with X is consistent with a single N, O, or C atom. We now have tested whether X is an N or not by comparing the Q-band ENDOR and ESEEM signals from resting-state (S = 3/2) MoFe protein and NMF-extracted FeMo-co from bacteria grown with either 14N or 15N as the exclusive N source. All of the 14N or 15N signals associated with the protein are lost upon extraction of the FeMo-co. We interpret this as strong evidence that X is not an N. Copyright © 2005 American Chemical Society.

引用

页码：12804 / 12805

页数：2

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