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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1978 Aug;75(8):3548–3550. doi: 10.1073/pnas.75.8.3548

Internal charge transfer in proteins to the Schiff bases of their lysine side chains

Peter Otto *, János Ladik *, Koloman Laki , Albert Szent-Györgyi
PMCID: PMC392820  PMID: 16592548

Abstract

Stereochemical investigations carried out with the aid of molecular models show that the Schiff bases formed between methylglyoxal and the primary amino groups of the lysine side chains of proteins can bend back in such a way to the N atoms of the peptide groups that a charge transfer can occur between these groups and the oxygen atoms of the Schiff bases. Ab initio molecular orbital calculations support this finding.

Keywords: methylglyoxal, lysine, peptide links, conductivity, electron acceptors

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bone S., Lewis T. J., Pethig R., Szent-Györgyi A. Electronic properties of some protein--methylglyoxal complexes. Proc Natl Acad Sci U S A. 1978 Jan;75(1):315–318. doi: 10.1073/pnas.75.1.315. [DOI] [PMC free article] [PubMed] [Google Scholar]
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