Interaction of HydSL hydrogenase from Thiocapsa roseopersicina with cyanide leads to destruction of iron-sulfur clusters
| Autor: | Nikolay A. Zorin, Alexey A. Zabelin, Anatoly A. Tsygankov, Anatoly Ya. Shkuropatov |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Iron-Sulfur Proteins Hydrogenase Absorption spectroscopy Cyanide Iron Inorganic chemistry chemistry.chemical_element Thiocapsa roseopersicina 010402 general chemistry Photochemistry 01 natural sciences Biochemistry Inorganic Chemistry 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins Catalytic Domain Spectroscopy Fourier Transform Infrared Fourier transform infrared spectroscopy Enzyme Inhibitors Cyanides biology Ligand Active site Sulfur 0104 chemical sciences 030104 developmental biology chemistry biology.protein Ferrocyanide Oxidation-Reduction |
| Zdroj: | Journal of inorganic biochemistry. 177 |
| ISSN: | 1873-3344 |
| Popis: | The effects of cyanide on enzymatic activity and absorption spectra in the visible and mid-IR (2150–1850 cm −1 ) regions were characterized for purified HydSL hydrogenase from the purple sulfur bacterium Thiocapsa (T.) roseopersicina BBS. Prolonged incubation (over hours) of T. roseopersicina hydrogenase with exogenous cyanide was shown to result in an irreversible loss of activity of the enzyme in both the oxidized (as isolated) and H 2 -reduced states. The frequency position of the active site CO and CN − ligand stretching bands in the Fourier transform infrared (FTIR) spectrum of the oxidized form of hydrogenase was not influenced by cyanide treatment. The 410-nm absorption band characteristic of hydrogenase iron‑sulfur clusters showed a bleaching concomitantly with cyanide inactivation. A new band at 2038 cm −1 was present in the FTIR spectrum of the cyanide-inactivated preparation, which band is assignable to ferrocyanide as a possible product of a destructive interaction of hydrogenase with cyanide. The results are interpreted in terms of a slow destruction of iron‑sulfur clusters of hydrogenase in the presence of cyanide accompanied by a release of iron ions in the form of ferrocyanide into the surrounding solution. Such a slow and irreversible cyanide-dependent inactivation seems to be complementary to a recently described rapid, reversible inhibitory reaction of cyanide with the active site of hydrogenases [S.V. Hexter, M.-W. Chung, K.A. Vincent, F.A. Armstrong, J. Am. Chem. Soc. 136 (2014) 10470–10477]. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect