Correlation Engine 2.0
Clear Search sequence regions

Sizes of these terms reflect their relevance to your search.

The ability of proteins to catalyze hydrogen evolution has been known for more than 80 years, but the poorly developed d.c. polarographic "pre-sodium wave" was of little analytical use. Recently, we have shown that by using constant current chronopotentiometric stripping analysis, proteins produce a well-developed peak H at hanging mercury drop and solid amalgam electrodes. Peak H sensitively reflects changes in protein structures due to protein denaturation, single amino acid exchange, etc. at the picomole level. Unmodified DNA and RNA do not yield such a peak, but they produce electrocatalytic voltammetric signals after modification with osmium tetroxide complexes with nitrogen ligands [Os(VIII)L], binding covalently to pyrimidine bases in nucleic acids. Recently, it has been shown that six-valent [Os(VI)L] complexes bind to 1,2-diols in polysaccharides and oligosaccharides, producing voltammetric responses similar to those of DNA-Os(VIII)L adducts. Electrocatalytic peaks produced by Os-modified nucleic acids, proteins (reaction with tryptophan residues) and carbohydrates are due to the catalytic hydrogen evolution, allowing determination of oligomers at the picomolar level. Copyright © 2012 The Japan Chemical Journal Forum and Wiley Periodicals, Inc.


Emil Paleček, Martin Bartošík, Veronika Ostatná, Mojmír Trefulka. Electrocatalysis in proteins, nucleic acids and carbohydrates. Chemical record (New York, N.Y.). 2012 Feb;12(1):27-45

Expand section icon Mesh Tags

Expand section icon Substances

PMID: 22287069

View Full Text