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  2. Histidine - Wikipedia

    en.wikipedia.org/wiki/Histidine

    Histidine ball and stick model spinning. Histidine (symbol His or H) [2] is an essential amino acid that is used in the biosynthesis of proteins.It contains an α-amino group (which is in the protonated –NH 3 + form under biological conditions), a carboxylic acid group (which is in the deprotonated –COO − form under biological conditions), and an imidazole side chain (which is partially ...

  3. Grotthuss mechanism - Wikipedia

    en.wikipedia.org/wiki/Grotthuss_mechanism

    Protons tunnel across a series of hydrogen bonds between hydronium ions and water molecules.. The Grotthuss mechanism (also known as proton jumping) is a model for the process by which an 'excess' proton or proton defect diffuses through the hydrogen bond network of water molecules or other hydrogen-bonded liquids through the formation and concomitant cleavage of covalent bonds involving ...

  4. Catalytic triad - Wikipedia

    en.wikipedia.org/wiki/Catalytic_triad

    Histidine is thus able to act as a powerful general base, activating the serine nucleophile. The histidine base aids the first leaving group by donating a proton, and also activates the hydrolytic water substrate by abstracting a proton as the remaining OH − attacks the acyl-enzyme intermediate. [23]

  5. Salt bridge (protein and supramolecular) - Wikipedia

    en.wikipedia.org/wiki/Salt_bridge_(protein_and...

    Continuing with the T4 lysozyme example, a titration curve is obtained through observation of a shift in the C2 proton of histidine 31 (Figure 5). Figure 5 shows the shift in the titration curve between the wild-type and the mutant in which Asp70 is Asn. The salt bridge formed is between the deprotonated Asp70 and protonated His31.

  6. Oxidative phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Oxidative_phosphorylation

    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 contribute to the proton gradient. The reaction catalyzed is the oxidation of cytochrome c and the reduction of oxygen:

  7. Acid catalysis - Wikipedia

    en.wikipedia.org/wiki/Acid_catalysis

    By Brønsted–Lowry acid–base theory, the acid is the proton (hydrogen ion, H +) donor and the base is the proton acceptor. Typical reactions catalyzed by proton transfer are esterifications and aldol reactions. In these reactions, the conjugate acid of the carbonyl group is a better electrophile than the neutral carbonyl group itself.

  8. Oxygen reduction reaction - Wikipedia

    en.wikipedia.org/wiki/Oxygen_reduction_reaction

    Rather than combustion, organisms rely on elaborate sequences of electron-transfer reactions, often coupled to proton transfer. The direct reaction of O 2 with fuel is precluded by the oxygen reduction reaction, which produces water and adenosine triphosphate. Cytochrome c oxidase affects the oxygen reduction reaction by binding O 2 in a heme ...

  9. Shuttle catalysis - Wikipedia

    en.wikipedia.org/wiki/Shuttle_catalysis

    Shuttle catalysis is used to describe catalytic reactions where a chemical entity of a donor molecule is transferred to an acceptor molecule. [1] In these reactions, while the number of chemical bonds of each reactant changes, the types and total number of chemical bonds remain constant over the course of the reaction.