Study of the mechanism of action of p-chloromercuribenzoate on endonuclease from the bacterium Serratia marcescens

Autor:	M N, Filimonova, V P, Gubskaya, I A, Nuretdinov, M J, Benedik, N A, Cherepanova, I B, Leshchinskaya
Rok vydání:	2001
Předmět:	Dose-Response Relationship Drug Ultraviolet Rays Cations Circular Dichroism p-Chloromercuribenzoic Acid Nucleic Acid Conformation Protein Isoforms Magnesium DNA Endonucleases Protein Structure Secondary Serratia marcescens Protein Binding
Zdroj:	Biochemistry. Biokhimiia. 66(3)
ISSN:	0006-2979
Popis:	The mechanism of action of p-chloromercuribenzoate (PCMB) on Serratia marcescens nuclease was investigated. The analysis showed that PCMB forms complexes with DNA. Binding of C7H5O2Hg+ to DNA changes the secondary structure of the DNA. These changes alter the enzymatic activity of S. marcescens nuclease, which was previously found to be sensitive to the secondary structure of the substrates. The nuclease activity was either suppressed or stimulated in the presence of PCMB depending on the C7H5O2Hg+ to nucleotide equivalent ratio. Binding of C7H5O2Hg+ to DNA did not form an abortive enzyme-substrate complex. Binding of Mg2+ to the C7H5O2Hg-DNA complex caused appropriate changes in secondary structure of the substrate. Since Mg2+ and C7H5O2Hg+, though differing in the type of metal cation, are similar in their mechanisms of influence on enzymatic activity of S. marcescens nuclease, the identity of other metal-containing effectors in their mechanism of action on Serratia marcescens nuclease is assumed.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::6a3a91c9913a290da5428ea10fcc2436 https://pubmed.ncbi.nlm.nih.gov/11333158 Zobrazit plný text záznamu Full text from SpringerLink