About the use of 13 C- 13 C NOESY in bioinorganic chemistry

Herein we present examples of the application of the C- C Nuclear Overhauser Effect Spectroscopy (NOESY) experiment to the study of metalloproteins and we critically discuss the advantages and drawbacks of the method as a function of the molecular size of the investigated systems. The contribution i...

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Bibliographic Details
Published in:Journal of inorganic biochemistry 2019-03, Vol.192, p.25
Main Authors: Ghini, Veronica, Chevance, Soizic, Turano, Paola
Format: Article
Language:English
Subjects:
Chemistry, Bioinorganic
Cytochromes c - chemistry
Ferritins - chemistry
Heme - chemistry
Humans
Male
Nuclear Magnetic Resonance, Biomolecular - methods
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Summary:Herein we present examples of the application of the C- C Nuclear Overhauser Effect Spectroscopy (NOESY) experiment to the study of metalloproteins and we critically discuss the advantages and drawbacks of the method as a function of the molecular size of the investigated systems. The contribution is focused on a few case studies among the systems analyzed in the group of the corresponding author. The C- C NOESY experiment represents the gold standard for the observation of NMR signals in the 480 kDa ferritin nanocage and for monitoring its interaction with iron. By decreasing the protein size, the experiment progressively loses its importance as a tool for the detection of the complete spin pattern of the amino acid side chains, as exemplified by nickel-dependent regulatory protein, NikR (molecular mass of the homo-tetramer ~80 kDa). In very small proteins, such as mitochondrial cytochrome c (12.3 kDa), we are only able to detect cross peaks between adjacent C nuclei; this feature turned out to be useful for the assignment of the C core resonances of the porphyrin in a uniformly enriched heme.
ISSN:1873-3344