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  2. 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]

  3. 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]

  4. Oxidative phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Oxidative_phosphorylation

    This enzyme mediates the final reaction in the electron transport chain and transfers electrons to oxygen and hydrogen (protons), while pumping protons across the membrane. [42] The final electron acceptor oxygen is reduced to water in this step. Both the direct pumping of protons and the consumption of matrix protons in the reduction of oxygen ...

  5. Cytochrome c oxidase - Wikipedia

    en.wikipedia.org/wiki/Cytochrome_c_oxidase

    The inability of the enzyme to reduce oxygen to water results in a buildup of oxygen, which can diffuse deeper into surrounding tissues. [25] NO inhibition of Complex IV has a larger effect at lower oxygen concentrations, increasing its utility as a vasodilator in tissues of need.

  6. Alternative oxidase - Wikipedia

    en.wikipedia.org/wiki/Alternative_oxidase

    The alternative oxidase is an integral monotopic membrane protein that is tightly bound to the inner mitochondrial membrane from matrix side [18] The enzyme has been predicted to contain a coupled diiron center on the basis of a conserved sequence motif consisting of the proposed iron ligands, four glutamate and two histidine amino acid residues. [19]

  7. Dioxygenase - Wikipedia

    en.wikipedia.org/wiki/Dioxygenase

    The most widely observed cofactor involved in dioxygenation reactions is iron, but the catalytic scheme employed by these iron-containing enzymes is highly diverse. Iron-containing dioxygenases can be subdivided into three classes on the basis of how iron is incorporated into the active site: those employing a mononuclear iron center, those containing a Rieske [2Fe-2S] cluster, and those ...

  8. Catalase - Wikipedia

    en.wikipedia.org/wiki/Catalase

    Catalase is a common enzyme found in nearly all living organisms exposed to oxygen (such as bacteria, plants, and animals) which catalyzes the decomposition of hydrogen peroxide to water and oxygen. [5] It is a very important enzyme in protecting the cell from oxidative damage by reactive oxygen species (ROS). Catalase has one of the highest ...

  9. Aerobic denitrification - Wikipedia

    en.wikipedia.org/wiki/Aerobic_denitrification

    The respiration reaction which utilizes oxygen as oxidant to produce energy from glucose is the following: C 6 H 12 O 6 (aq) + 6 O 2 (g) → 6 CO 2 (g) + 6 H 2 O. Classically, it was thought that denitrification would not occur in the presence of oxygen since there seems to be no energetic advantage to using nitrate as an oxidant when oxygen is ...