MXAN Analysis of the XANES Energy Region of LiPDF

GUO Xiao-Yun; CHU Wang-Sheng; GONG Wei-Min; DONG Yu-Hui; XIE Ya-Ning; YANG Fei-Fei; Maurizio Benfatto; WU Zi-Yu

Chinese Physics C> 2007, Vol. 31> Issue(2) : 199-203

MXAN Analysis of the XANES Energy Region of LiPDF

School of Life Science,University of Science and Technology of China, Hefei 230026, China2 Institute of High Energy Physics, CAS, Beijing 100049, China3 National Laboratory of Biomacromolecules, Institute of Biophysics,Chinese Academy of Sciences, Beijing 100101, China4 Instituto Nazionale di Fisica Nucleare, Laboratori Nazionali di Frascati, P.O. Box 13, 00044, Frascati, Italy

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Abstract：
Leptospira interrogans peptide deformylase (LiPDF) is an important Zinc metalloprotein and plays a key role in protein synthesis of Leptospira interrogans, an ubiquitous environmental bacterium that can cause the infections of animals and humans. It is an attractive target for the design of new antibiotics since the deformyling apparently does not occur in the cytoplasm of eucaryotic cells. In this paper, we probed the protein in pH3.0 solution by X-ray absorption near-edge structure (XANES) spectroscopy. We quantitatively determined the local structure around the metal center using MXAN procedure, which is based on Multiple Scattering theory. The experimental XANES spectrum of LiPDF has been reconstructed perfectly using suitable initial structure mode, and the corresponding local structure of the active center provides structure information for understanding the pH-dependent enzymatic activity.

References

[1]

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GUO Xiao-Yun, CHU Wang-Sheng, GONG Wei-Min, DONG Yu-Hui, XIE Ya-Ning, YANG Fei-Fei, Maurizio Benfatto and WU Zi-Yu. MXAN Analysis of the XANES Energy Region of LiPDF[J]. Chinese Physics C, 2007, 31(2): 199-203.

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Received: 2006-05-17
Revised: 2006-05-23

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通讯作者: 陈斌, bchen63@163.com

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沈阳化工大学材料科学与工程学院沈阳 110142

MXAN Analysis of the XANES Energy Region of LiPDF

Corresponding author: Maurizio Benfatto,

School of Life Science,University of Science and Technology of China, Hefei 230026, China2 Institute of High Energy Physics, CAS, Beijing 100049, China3 National Laboratory of Biomacromolecules, Institute of Biophysics,Chinese Academy of Sciences, Beijing 100101, China4 Instituto Nazionale di Fisica Nucleare, Laboratori Nazionali di Frascati, P.O. Box 13, 00044, Frascati, Italy

Received Date: 2006-05-17

Accepted Date: 2006-05-23

Available Online: 2007-02-05

Abstract: Leptospira interrogans peptide deformylase (LiPDF) is an important Zinc metalloprotein and plays a key role in protein synthesis of Leptospira interrogans, an ubiquitous environmental bacterium that can cause the infections of animals and humans. It is an attractive target for the design of new antibiotics since the deformyling apparently does not occur in the cytoplasm of eucaryotic cells. In this paper, we probed the protein in pH3.0 solution by X-ray absorption near-edge structure (XANES) spectroscopy. We quantitatively determined the local structure around the metal center using MXAN procedure, which is based on Multiple Scattering theory. The experimental XANES spectrum of LiPDF has been reconstructed perfectly using suitable initial structure mode, and the corresponding local structure of the active center provides structure information for understanding the pH-dependent enzymatic activity.

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MXAN Analysis of the XANES Energy Region of LiPDF

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