Results 311 to 320 of about 175,409 (339)
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OXYGENASES

1974
Publisher Summary This chapter reviews the reaction mechanisms of iron-containing oxygenases with a special emphasis on the role of iron in the function and structure of oxygenases. The role of iron in oxygenases has been assumed to be a site of oxygen activation but also appears to be closely related to the substrate binding site, although the ...
MITSUHIRO NOZAKI, YUZURU ISHIMURA
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Bacterial Heme Oxygenases

Antioxidants & Redox Signaling, 2004
The importance of heme oxygenases in heme catabolism, iron utilization, and cellular signaling has been recognized for many years and is a well studied process in eukaryotes. Through the accessibility of an increasing number of bacterial genomes, it has become evident that heme oxygenases are also widespread in prokaryotes. In these organisms, the heme
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Heme oxygenase-1 and heme oxygenase-2 expression in bruises

Forensic Science, Medicine, and Pathology, 2015
The first step in catabolism of hemoglobin in a bruise is performed by the enzyme heme oxygenase, which produces biliverdin that is then reduced to bilirubin. The development of yellow coloration in bruises can be attributed to local accumulation of degradation products of hemoglobin, including bilirubin, but it is not clear why there is a delay before
Claire G. Ross   +3 more
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The mechanism of heme oxygenase

Current Opinion in Chemical Biology, 2000
Major advances have been made in determining the structure of heme oxygenase and the relationship between its structure and catalytic activity. The nature of the first step in the reaction sequence, heme alpha-meso-hydroxylation, is now clear, although the mechanisms that control the alpha-regiospecificity remain elusive. Hypothetical mechanisms can be
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Analgesia and cyclo-oxygenase inhibitors

Digestive and Liver Disease, 2001
Non-steroidal anti-inflammatory drugs are among the most commonly used medications and they are a mainstay in the treatment of inflammatory diseases. Non-steroidal anti-inflammatory drugs are widely used to reduce pain associated with acute or chronic inflammation.
MELI, ROSARIA   +2 more
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Oxidases and Oxygenases

2007
An oxidase catalyzes the oxidation of a substrate by O2 without incorporating an oxygen atom into the product. A monooxygenase catalyzes oxidation by O2 with incorporation of one oxygen atom into the product, and oxidation by a dioxygenase proceeds with incorporation of both atoms of O2 into the product.
Perry A. Frey, Adrian D. Hegeman
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Cofactor-independent oxidases and oxygenases

Applied Microbiology and Biotechnology, 2010
Whereas the majority of O(2)-metabolizing enzymes depend on transition metal ions or organic cofactors for catalysis, a significant number of oxygenases and oxidases neither contain nor require any cofactor. Among the cofactor-independent oxidases, urate oxidase, coproporphyrinogen oxidase, and formylglycine-generating enzyme are of mechanistic as well
Fetzner S., Steiner R.
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Practical issues in the application of oxygenases

Trends in Biotechnology, 2003
Oxygenases carry out the regio-, stereo- and chemoselective introduction of oxygen in a tremendous range of organic molecules. This versatility has already been exploited in several commercial processes. There are, however, many hurdles to further practical large-scale applications.
Wouter A. Duetz   +3 more
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Oxidoreductases and Oxygenases

1984
Oxidoreductases (dehydrogenases or oxidases) catalyze the addition or the removal of hydrogen or electrons. Oxygenases bring about the incorporation of oxygen which originates from molecular oxygen.
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Heme Oxygenase-1 [PDF]

open access: possible, 2002
Oxidative stresses such as oxidant stimuli, inflammation, exposure to xenobiotics, and ionizing irradiation elicit various tissue injuries and provoke cellular responses, principally involving transcriptional activation of genes encoding proteins which participate in the defense reactions (Camhi et al., 1995).
Reiko Akagi   +4 more
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