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
Full text
PDF


Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- 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]
- Pethig R., Szent-Györgyi A. Electronic properties of the casein-methylglyoxal complex. Proc Natl Acad Sci U S A. 1977 Jan;74(1):226–228. doi: 10.1073/pnas.74.1.226. [DOI] [PMC free article] [PubMed] [Google Scholar]