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  2. Denaturation (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Denaturation_(biochemistry)

    In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]

  3. Pasteur effect - Wikipedia

    en.wikipedia.org/wiki/Pasteur_effect

    First, glucose metabolism is faster through ethanol fermentation because it involves fewer enzymes and limits all reactions to the cytoplasm. Second, ethanol has bactericidal activity by causing damage to the cell membrane and protein denaturing, allowing yeast fungus to outcompete environmental bacteria for resources. [6]

  4. Oxidative phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Oxidative_phosphorylation

    Oxidative phosphorylation uses these molecules and O 2 to produce ATP, which is used throughout the cell whenever energy is needed. During oxidative phosphorylation, electrons are transferred from the electron donors to a series of electron acceptors in a series of redox reactions ending in oxygen, whose reaction releases half of the total ...

  5. Nitric-oxide reductase - Wikipedia

    en.wikipedia.org/wiki/Nitric-oxide_reductase

    Nitric oxide reductase was assigned Enzyme Commission number (EC) 1.7.2.5. Enzyme Commission numbers are the standard naming system used for enzymes. [5] The EC identifies the class, subclass, sub-subclass, and serial number of the enzyme. [5] Nitric oxide reductase is in Class 1, therefore it is an oxidoreductases. [5] Figure 1. The Nitrogen ...

  6. Nitrate reductase - Wikipedia

    en.wikipedia.org/wiki/Nitrate_reductase

    The active site of these enzymes is a molybdenum ion that is bound to the four thiolate functional groups of two pterin molecules. The coordination sphere of the molybdenum ion is completed by one amino-acid side chain and oxygen and/or sulfur ligands. In Nap, the molybdenum is covalently attached to the protein by a cysteine side chain, and an ...

  7. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    Exopeptidase enzymes exist in the small intestine. These enzymes have two classes: aminopeptidases are a brush border enzyme and carboxypeptidases which is from the pancreas. Aminopeptidases are enzymes that remove amino acids from the amino terminus of protein. They are present in all lifeforms and are crucial for survival since they do many ...

  8. Oxidoreductase - Wikipedia

    en.wikipedia.org/wiki/Oxidoreductase

    For example, an enzyme that catalyzed this reaction would be an oxidoreductase: A – + B → A + B – In this example, A is the reductant (electron donor) and B is the oxidant (electron acceptor). In biochemical reactions, the redox reactions are sometimes more difficult to see, such as this reaction from glycolysis:

  9. Beta oxidation - Wikipedia

    en.wikipedia.org/wiki/Beta_oxidation

    The enzyme catalase, found primarily in peroxisomes and the cytosol of erythrocytes (and sometimes in mitochondria [12]), converts the hydrogen peroxide into water and oxygen. Peroxisomal β-oxidation also requires enzymes specific to the peroxisome and to very long fatty acids.