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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-7565-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-7566-A
Genre: Journal Article
Alternative Title : Isolation and crystallization of functionally competent Escherichia coli peptide deformylase forms containing either iron or nickel in the active site

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BiochemBiophysResComm_246_1998_342.pdf (Any fulltext), 112KB
 
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 Creators:
Groche, Dieter, Author
Becker, Andreas1, Author              
Schlichting, Ilme1, Author              
Kabsch, Wolfgang1, 2, Author              
Schultz, Sabine, Author
Wagner, A. F. Volker, Author
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 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.

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Language(s): eng - English
 Dates: 1998-04-101998-05-19
 Publication Status: Published in print
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
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Title: Biochemical and Biophysical Research Communications
  Other : Biochem. Biophys. Res. Commun.
Source Genre: Journal
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Publ. Info: Orlando, Fla. : Academic Press
Pages: - Volume / Issue: 246 (2) Sequence Number: - Start / End Page: 342 - 346 Identifier: ISSN: 0006-291X
CoNE: https://pure.mpg.de/cone/journals/resource/954922652205_1