Direct probe of iron vibrations elucidates NO activation of heme proteins

被引：43

作者：

Zeng, WQ

Silvernail, NJ

Wharton, DC

Georgiev, GY

Leu, BM

Scheidt, WR

Zhao, JY

Sturhahn, W

Alp, EE

Sage, JT ^{[1
]}

机构：

[1] Northeastern Univ, Dept Phys, Boston, MA 02115 USA

[2] Northeastern Univ, Ctr Interdisciplinary Res Complex Syst, Boston, MA 02115 USA

[3] Argonne Natl Lab, Adv Photon Source, Argonne, IL 60439 USA

[4] Univ Notre Dame, Dept Chem & Biochem, Notre Dame, IN 46556 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2005年 / 127卷 / 32期

关键词：

D O I：

10.1021/ja051052x

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

We use nuclear resonance vibrational spectroscopy (NRVS) to identify the Fe-NO stretching frequency in the NO adduct of myoglobin (MbNO) and in the related six-coordinate porphyrin Fe(TPP)(1-MeIm)(NO). Frequency shifts observed in MbNO Raman spectra upon isotopic substitution of Fe or the nitrosyl nitrogen confirm and extend the NRVS results. In contrast with previous assignments, the Fe-NO frequency of these six-coordinate complexes lies 70-100 cm-1 lower than in the analogous five-coordinate nitrosyl complexes, indicating a significant weakening of the Fe-NO bond in the presence of a trans imidazole ligand. This result supports proposed mechanisms for NO activation of heme proteins and underscores the value of NRVS as a direct probe of metal reactivity in complex biomolecules. Copyright © 2005 American Chemical Society.

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页码：11200 / 11201

页数：2

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