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If the area of inoculation turns dark-blue to maroon to almost black, then the result is positive. If a color change does not occur within three minutes, the result is negative. In alternative manner, live bacteria cultivated on trypticase soy agar plates may be prepared using sterile technique with a single-line streak inoculation. The ...
In reactions involving donation of a hydrogen atom, oxygen is reduced to water (H 2 O) or hydrogen peroxide (H 2 O 2). Some oxidation reactions, such as those involving monoamine oxidase or xanthine oxidase, typically do not involve free molecular oxygen. [1] [2] The oxidases are a subclass of the oxidoreductases. The use of dioxygen is the ...
Two types of oxygenases are recognized: Monooxygenases, or mixed function oxidase, transfer one oxygen atom to the substrate, and reduce the other oxygen atom to water. Dioxygenases, or oxygen transferases, incorporate both atoms of molecular oxygen (O 2) into the product(s) of the reaction. [3]
Squalene monooxygenase (also called squalene epoxidase) is a eukaryotic enzyme that uses NADPH and diatomic oxygen to oxidize squalene to 2,3-oxidosqualene (squalene epoxide). Squalene epoxidase catalyzes the first oxygenation step in sterol biosynthesis and is thought to be one of the rate-limiting enzymes in this pathway. [5]
NAD + to NADH. FMN to FMNH 2. CoQ to CoQH 2.. Complex I is the first enzyme of the mitochondrial electron transport chain.There are three energy-transducing enzymes in the electron transport chain - NADH:ubiquinone oxidoreductase (complex I), Coenzyme Q – cytochrome c reductase (complex III), and cytochrome c oxidase (complex IV). [1]
In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule, the reductant, also called the electron donor, to another, the oxidant, also called the electron acceptor. This group of enzymes usually utilizes NADP+ or NAD+ as cofactors.
HO-2 is encoded by the HMOX2 gene. HO-2 is 36 kDa and shares 47% similarity with the HO-1 amino acid sequence; notably HO-2 has an extra N-terminal stretch of 20 amino acid residues. [5] Unlike HO-1, HO-2 is a hemoprotein containing heme regulatory motifs that contain heme independent of the heme catabolic site. [3]
Ceruloplasmin EC 1.16.3.1 (ferroxidase), a 6-domain enzyme found in the serum of mammals and birds that oxidizes different inorganic and organic substances; exhibits internal sequence homology that appears to have evolved from the triplication of a Cu-binding domain similar to that of laccase and ascorbate oxidase. Laccase EC 1.10.3.2 (urishiol ...