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The structure of the periplasmic nickel-binding protein NikA provides insights for artificial metalloenzyme design

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The structure of the periplasmic nickel-binding protein NikA provides insights for artificial metalloenzyme design

Content Provider	Springer Nature Link
Author	Cherrier, Mickaël V. Girgenti, Elodie Amara, Patricia Iannello, Marina Marchi Delapierre, Caroline Fontecilla Camps, Juan C. Ménage, Stéphane Cavazza, Christine
Copyright Year	2012
Abstract	Understanding the interaction of a protein with a relevant ligand is crucial for the design of an artificial metalloenzyme. Our own interest is focused on the synthesis of artificial monooxygenases. In an initial effort, we have used the periplasmic nickel-binding protein NikA from Escherichia coli and iron complexes in which N2Py2 ligands (where Py is pyridine) have been varied in terms of charge, aromaticity, and size. Six “NikA/iron complex” hybrids have been characterized by X-ray crystallography, and their interactions and solution properties have been studied. The hybrids are stable as indicated by their K d values, which are all in the micromolar range. The X-ray structures show that the ligands interact with NikA through salt bridges with arginine residues and π-stacking with a tryptophan residue. We have further characterized these interactions using quantum mechanical calculations and determined that weak CH/π hydrogen bonds finely modulate the stability differences between hybrids. We emphasize the important role of the tryptophan residues. Thus, our study aims at the complete characterization of the factors that condition the interaction of an artificial ligand and a protein and their implications for catalysis. Besides its potential usefulness in the synthesis of artificial monooxygenases, our approach should be generally applicable in the field of artificial metalloenzymes.
Starting Page	817
Ending Page	829
Page Count	13
File Format	PDF
ISSN	09498257
Journal	JBIC Journal of Biological Inorganic Chemistry
Volume Number	17
Issue Number	5
e-ISSN	14321327
Language	English
Publisher	Springer-Verlag
Publisher Date	2012-04-21
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Artificial metalloenzyme Ligand binding X-ray crystallography Iron chemistry CH/π bonds Microbiology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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