nitrite oxidoreductase β Inhibitors
Nitrite oxidoreductase β inhibitors are a class of chemical compounds that specifically target and inhibit the β-subunit of nitrite oxidoreductase enzymes. These enzymes play a central role in the biogeochemical nitrogen cycle by catalyzing the oxidation of nitrite (NO₂⁻) to nitrate (NO₃⁻), a crucial step in the nitrogen transformation process. Nitrite oxidoreductase is a multi-subunit enzyme complex, and the β-subunit is particularly significant for its role in electron transfer during the oxidation process. Inhibition of this subunit disrupts the electron flow necessary for the redox reactions that occur within the enzyme complex, thereby impeding the overall oxidation of nitrite. The specificity of inhibitors targeting the β-subunit makes them valuable tools for probing the function and regulation of nitrite oxidation pathways in both environmental and biochemical systems.
These inhibitors provide key insights into the structural and functional mechanisms of nitrite oxidoreductase complexes, especially in microorganisms such as nitrifying bacteria. By studying how β-subunit inhibitors affect nitrite oxidation, researchers can better understand the enzyme's kinetics and interaction with various cofactors and substrates. In some cases, these inhibitors are also used to study the broader metabolic consequences of disrupting nitrite oxidation, as this process is intricately linked to other microbial pathways involved in energy production and nitrogen metabolism. Through targeted inhibition of the β-subunit, scientists can further elucidate the dynamics of nitrogen cycling in natural ecosystems and in engineered environments where nitrification plays an essential role.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Sodium chlorate | 7775-09-9 | sc-212938 | 100 g | $58.00 | 1 | |
Sodium chlorate may outcompete nitrite for the active site of nitrite oxidoreductase β, thereby potentially downregulating the enzyme's expression by creating a negative feedback loop that signals reduced need for the enzyme due to apparent substrate excess. | ||||||
Sodium azide | 26628-22-8 | sc-208393 sc-208393B sc-208393C sc-208393D sc-208393A | 25 g 250 g 1 kg 2.5 kg 100 g | $42.00 $152.00 $385.00 $845.00 $88.00 | 8 | |
Sodium azide may decrease the expression of nitrite oxidoreductase β by disrupting the electron transport chain, leading to energy deficits that could trigger a conservation response, reducing the synthesis of energy-intensive proteins like nitrite oxidoreductase β. | ||||||
Cobalt(II) chloride | 7646-79-9 | sc-252623 sc-252623A | 5 g 100 g | $63.00 $173.00 | 7 | |
Cobalt(II) chloride could inhibit the expression of nitrite oxidoreductase β by competing with necessary metal cofactors, potentially leading to improper enzyme assembly and signaling for reduced production of the misassembled enzyme. | ||||||
Dimethyl Sulfoxide (DMSO) | 67-68-5 | sc-202581 sc-202581A sc-202581B | 100 ml 500 ml 4 L | $30.00 $115.00 $900.00 | 136 | |
Dimethyl sulfoxide might permeabilize bacterial membranes, leading to ionic imbalances that could decrease the expression of nitrite oxidoreductase β due to disrupted cell homeostasis and defense prioritization. | ||||||
Atrazine | 1912-24-9 | sc-210846 | 5 g | $165.00 | 1 | |
Atrazine may indirectly reduce the expression of nitrite oxidoreductase β by inhibiting photosynthesis in aquatic environments, reducing the availability of organic compounds for nitrifying bacteria, and thus diminishing their population and the enzymes they express. | ||||||
Copper(II) sulfate | 7758-98-7 | sc-211133 sc-211133A sc-211133B | 100 g 500 g 1 kg | $45.00 $120.00 $185.00 | 3 | |
Copper(II) sulfate in high concentrations could bind to the active sites of enzymes or displace other metal ions, potentially leading to a decrease in the active enzyme and a signal for the downregulation of nitrite oxidoreductase β expression. | ||||||
Zinc | 7440-66-6 | sc-213177 | 100 g | $47.00 | ||
Zinc sulfate, when present in excess, might inhibit enzyme activity by competing with other necessary metal ions for binding sites, potentially resulting in a conformational change of the enzyme that leads to its decreased expression. | ||||||