reductases การใช้
- Novel nitrite reductases have been isolated from strains of this species.
- Most oxidases and reductases are proton pumps, but some are not.
- Class III reductases are distributed in archaebacteria, eubacteria, and bacteriophages.
- Trypanothione-dependent enzymes include reductases, peroxidases, glyoxalases and transferases.
- It is also used in biochemical experiments as an inhibitor of reductases.
- This flexibility is possible because different oxidases and reductases use the same ubiquinone pool.
- Class I reductases are divided into IA and IB due to differences in regulation.
- Siroheme is a co-factor of both assimilatory and dissimilatory nitrite and sulfite reductases.
- Most of the photosynthetic bacteria have both light-dependent and light-independent reductases.
- Class IA reductases are distributed in eukaryotes, S-adenosyl methionine and an iron sulphur center.
- It has also been suggested that flavin reductases play a role in the production of hydrogen peroxide.
- RT-qPCR studies revealed that genes coding for both heterodisulfide reductases were expressed at high levels.
- Class I reductases use an iron center with ferrous to ferric conversion to generate a tyrosyl free radical.
- Some ( very few ) mercuric ( II ) reductases have been found to lack the NmerA domain.
- Ferredoxin NADP reductases are present in many organisms, including plants, bacteria, and the mitochondria of eukaryotes.
- The " Pseudomonas aeruginosa " genome has separate genes for glutaredoxin-and thioredoxin-coupled ArsC reductases.
- Eukaryotic cells with class IA reductases have a mechanism of negative control to turn off synthesis of dNTPs as they accumulate.
- Sulfite reductases belong to the family of oxidoreductases, and are found in archaea, bacteria, fungi, and plants.
- In her current research, Stubbe continues to study the function of ribonucleotide reductases and the mechanisms of clinically useful drugs.
- Anaerobic bacteria, which do not use oxygen as a terminal electron acceptor, have terminal reductases individualized to their terminal acceptor.
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