EC Number   |
Inhibitors |
Structure |
|---|
  1.8.5.8 | 2-ethoxy-4-(4-fluorophenyl)-5H-indeno[1,2-b]pyridine-3-carbonitrile |
HTS12441 |
 |
| 1.8.5.8 | 2-methoxy-4-phenyl-5H-indeno[1,2-b]pyridine-3-carbonitrile |
RH00520 |
|
| 1.8.5.8 | 4-(2-chlorophenyl)-2-methoxy-5H-indeno[1,2-b]pyridine-3-carbonitrile |
HTS12442 |
|
| 1.8.5.8 | 4-(4-aminophenyl)-6-methoxy-3'-methyl[2,2'-bipyridine]-5-carbonitrile |
STI1, SQOR-targeted inhibitor 1, STI1 is a potent and highly selective inhibitor of SQOR. The first-in-class inhibitor of sulfide:quinone oxidoreductase binds to the CoQ-binding pocket in human SQOR and protects against adverse cardiac remodeling and heart failure. Ability of STI1 to protect against pathological remodelling of the left ventricle and the progression to heart failure patients with reduced ejection fraction (HFrEF). Docking of STI1 to ligand-free SQOR (PDB ID 6M06) and modeling of the SQOR-STI1 complex |
|
| 1.8.5.8 | 4-(4-aminophenyl)-6-methoxy-3'-methyl[2,2'-bipyridine]-5-carbonitrile |
STI1, SQOR-targeted inhibitor 1, STI1 is a potent and highly selective inhibitor of SQOR. The first-in-class inhibitor of sulfide:quinone oxidoreductase binds to the CoQ-binding pocket in SQOR and protects against adverse cardiac remodeling and heart failure |
|
| 1.8.5.8 | 4-(4-aminophenyl)-6-methoxy-3'-methyl[2,2'-bipyridine]-5-carbonitrile |
STI1, SQOR-targeted inhibitor 1, STI1 is a potent and highly selective inhibitor of SQOR. STI1 is a competitive inhibitor that binds with high selectivity to the coenzyme Q-binding pocket in SQOR. STI1 exhibits very low cytotoxicity and attenuats the hypertrophic response of neonatal rat ventricular cardiomyocytes and H9c2 cells induced by neurohormonal stressors |
|
| 1.8.5.8 | cyanide |
cyanide treatment destabilized human SQOR and leads to its inactivation with concomitant loss of the bridging sulfane sulfur. Addition of sulfide to inactive cyanide treated enzyme leads to recovery of active SQOR, indicating that the oxidation state of the active site cysteines is preserved upon cyanide treatment. Crystallization of SQOR with cyanide led to the capture of a 379Cys N-(201Cys-disulfanyl)-methanimido thioate intermediate. Spectral and kinetic characterization of cyanolysis-induced dismantling followed by sulfide-dependent rebuilding of the trisulfide cofactor, proposed mechanism for cyanolysis and cysteine trisulfide rebuilding in SQOR, overview |
  |
| 1.8.5.8 | ethyl [(3-cyano-4,6-diphenylpyridin-2-yl)oxy]acetate |
HTS07545 |
|
| 1.8.5.8 | H2S |
the enzyme activity decreases when the ambient sulfide concentration exceeds 0.3 mM |
|
| 1.8.5.8 | more |
not inhibited by up to 2 mM H2S |
|
