Stigmatellinum is a potent inhibitor of the quinol oxidation site (Q out site) of the cytochrome bc 1 complex of mitochondria and the cytochrome b 6 f complex in the thylakoid membrane .
| Stigmatellin | |
|---|---|
 | |
| Are common | |
| Chem. formula | C 30 H 42 O 7 |
| Physical properties | |
| Molar mass | 514.65 g / mol |
| Classification | |
| Reg. CAS number | 91682-96-1 |
| PubChem | |
| Reg. EINECS number | |
| Smiles | |
| Inchi | |
| Chebi | 32155 |
| ChemSpider | |
Stigmatellin was isolated from myxobacterium Stigmatella aurantica and contains a 5,7-dimethoxy-8-hydroxychromone aromatic group with an alkene chain in the second position. Structures of bc 1 complexes of bovine and yeast ( Saccharomyces cerevisiae ) inhibited by stigmatellin were obtained. It binds to the Q out site of cytochrome b distal to heme b L and interacts with the histidine residue (His-181) of the Riske protein via a hydrogen bond. This histidine residue serves as a ligand for the iron-sulfur cluster [2Fe-2S]. The hydrogen bond increases the redox potential of the iron-sulfur cluster from 290 to 540 mV and fetters the movement of the Beliske cytoplasmic domain [1] .
Notes
- ↑ Gurung Buddha , Yu Linda , Yu Chang-An. Stigmatellin Induces Reduction of Iron-Sulfur Protein in the Oxidized Cytochromebc1Complex // Journal of Biological Chemistry. - 2008. - August 13 ( t. 283 , No. 42 ). - S. 28087-28094 . - ISSN 0021-9258 . - DOI : 10.1074 / jbc.M804229200 .
Literature
- von Jagow, G., and Link, TA Methods in Enzymology 126: 253–271 (1986)