Direct Evidence for Ferrous Ion Oxidation and Incorporation in the Absence of Oxidants by Dps from Marinobacter hydrocarbonoclasticus.
Daniela PenasAlice S PereiraPedro TavaresPublished in: Angewandte Chemie (International ed. in English) (2018)
Dps proteins (DNA-binding protein from starved cells) are hollow-sphere-shaped, dodecameric enzymes found in bacteria and archaeal species. They can oxidize ferrous iron in a controlled manner using hydrogen peroxide or molecular oxygen as co-substrate, and most of them confer physical protection through DNA binding. Oxidized iron is stored, as a mineral core, in a central cavity. Direct evidence is now provided that, furthermore, Dps proteins containing small mineral cores can oxidize and mineralize toxic ferrous ions in anaerobic conditions and in the absence of any additional aqueous oxidant co-substrate. Dps proteins containing cores of 24 irons per dodecamer can oxidize about 5 ferrous irons per dodecamer, with that number approximately doubling for protein particles containing in average 96 irons per protein. This additional activity carries importance as it can be a detoxification mechanism present during anaerobic or oxygen-limited growth conditions.
Keyphrases
- hydrogen peroxide
- binding protein
- dna binding
- microbial community
- wastewater treatment
- amino acid
- nitric oxide
- induced apoptosis
- protein protein
- transcription factor
- physical activity
- single molecule
- sewage sludge
- cell cycle arrest
- cell free
- risk assessment
- cell death
- ionic liquid
- room temperature
- iron deficiency
- high resolution
- anti inflammatory
- oxidative stress
- heavy metals