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Enzyme Activity Measurement for Oxidoreductases Interacting with Inorganics

Creative Enzymes has demonstrated outstanding techniques in enzyme activity assays over the past decade. Our unique advantage in assay services is established on the foundation of constant acquisition and development of knowledge and methods in enzymology. In addition to regular activity assays, we also developed quantification methods specifically for uncommon oxidoreductases that have not been well characterized, such as oxidoreductases interacting with inorganic donors or acceptors.

The promising potential applications of oxidoreductases in biotechnology and drug discovery have been well recognized due to their instrumental functions in metabolism, cell signaling, and genetic regulations. The idea is widely accepted that the enzymes act on key intermediate and signaling molecules, which are nearly all organic molecules. However, many other oxidoreductases also employ inorganic chemicals, as electron donors or acceptors. They are at least equally important as the enzyme that act on organic chemicals, but often neglected. For example, the catalase enzyme uses hydrogen peroxide as the electron acceptor and is the key catalyst that converts some prodrugs into active drugs to treat infectious diseases. Superoxide reductase (EC 1.15) is indispensable in removing the toxic superoxide species into less toxic hydrogen peroxide, which is further reduced by peroxidases (EC 1.11) to nontoxic molecules. Similarly, sulfur dioxygenase participates in detoxification in humans. Notably, although these enzymes use inorganic molecules as donors or accepters, many of them also act on organic substrates, such as lipoxygenase which adds a molecule of oxygen onto fatty acids and is important in cell signaling. In archaea and bacteria, EC 1.16 oxidoreductases are necessary for the microorganisms to utilize metal ions as an energy source. Recently, the properties have attracted research interests for potential environmental applications, such as redemption of soil and water contaminated with heavy metals.

As environmental concerns and needs in new material are continuously rising, the number of studies of these oxidoreductases also grow fast to explore the potential use in environment protection and synthesis of new materials. Nonetheless, the catalytic mechanisms and enzyme kinetics remain unclear for many of these enzymes, partially because the natural substrates are either not easily available or not compatible with traditional measurement and detection methods. To solve the issues, Creative Enzymes focused on innovative detection and quantification approaches and demonstrated accurate and reliable activity determination methods on most of these enzymes. We are able to yield precise and reproducible results upon requests of regular enzyme activity tests, as well as special needs of activity assays for rare enzymes or enzymes under unusual reaction conditions. Up till now, the excellent quality of services has been endorsed by thousands of clients of Creative Enzymes. We are excited to expand our business to more regions and reach out to researchers in many different fields. Your test requests will be handled professionally and fulfilled with satisfaction.

 The crystal structure of a single monomer of the I. hospitalis superoxide reductase, showing the iron ion in blue sphere. Figure: The crystal structure of a single monomer of the I. hospitalis superoxide reductase, showing the iron ion in blue sphere.
Reference: Horch, M. et al., “Reductive activation and structural rearrangement in superoxide reductase: a combined infrared spectroscopic and computational study”, Phys. Chem. Chem. Phys., (2014) 16, 14220-14230.

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