Isolation and crystallization of functionally competent Escherichia coli 
peptide deformylase forms containing either iron or nickel in the active site

Groche, Dieter; Becker, Andreas; Schlichting, Ilme; Kabsch, Wolfgang; Schultz, Sabine; Wagner, A. F. Volker

doi:10.1006/bbrc.1998.8616

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Isolation and crystallization of functionally competent Escherichia coli peptide deformylase forms containing either iron or nickel in the active site

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Becker, Andreas
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Schlichting, Ilme
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Kabsch, Wolfgang
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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http://www.sciencedirect.com/science/article/pii/S0006291X98986168/pdf?md5=efa1b5be6260f074417ad0f63ca0b2b5&pid=1-s2.0-S0006291X98986168-main.pdf
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Citation

Groche, D., Becker, A., Schlichting, I., Kabsch, W., Schultz, S., & Wagner, A. F. V. (1998). Isolation and crystallization of functionally competent Escherichia coli peptide deformylase forms containing either iron or nickel in the active site. Biochemical and Biophysical Research Communications, 246(2), 342-346. doi:10.1006/bbrc.1998.8616.

Cite as: https://hdl.handle.net/11858/00-001M-0000-002B-7565-C

Abstract

Three metallo forms of peptide deformylase (PDF, EC 3.5.1.31) of Escherichia coli were prepared and crystallized (space group C2, diffraction limit 1.9 A) for initiating the X-ray structure determination of the metal center in correlation with the catalytic functionality of this enzyme. The native Fe2+ containing enzyme species was directly isolated from overproducing bacteria by using catalase as a buffer additive, which stabilizes the catalytic activity against oxidative destruction. The Ni2+ containing form, which is oxygen-insensitive, was obtained by metal exchange with free Ni2+ and found to be catalytically equally effective (kcat/KM = 10(5) M-1 s-1 for N-formyl-Met-Ala). The Zn2+ form, prepared from the apoenzyme or by displacement of bound Ni2+ by free Zn2+, proved virtually inactive.