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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. Catalytic triad - Wikipedia

    en.wikipedia.org/wiki/Catalytic_triad

    The endothelial protease vasohibin [f] uses a cysteine as the nucleophile, but a serine to coordinate the histidine base. [43] [44] Despite the serine being a poor acid, it is still effective in orienting the histidine in the catalytic triad. [43] Some homologues alternatively have a threonine instead of serine at the acid location. [43]

  4. 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.

  5. Proton pump - Wikipedia

    en.wikipedia.org/wiki/Proton_pump

    In cell respiration, the proton pump uses energy to transport protons from the matrix of the mitochondrion to the inter-membrane space. [1] It is an active pump that generates a proton concentration gradient across the inner mitochondrial membrane, because there are more protons outside the matrix than inside.

  6. 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 ...

  7. Nicotinamide adenine dinucleotide - Wikipedia

    en.wikipedia.org/wiki/Nicotinamide_adenine_di...

    The proton is released into solution, while the reductant RH 2 is oxidized and NAD + reduced to NADH by transfer of the hydride to the nicotinamide ring. RH 2 + NAD + → NADH + H + + R; From the hydride electron pair, one electron is attracted to the slightly more electronegative atom of the nicotinamide ring of NAD + , becoming part of the ...

  8. His-tag - Wikipedia

    en.wikipedia.org/wiki/His-tag

    A polyhistidine-tag, best known by the trademarked name His-tag, is an amino acid motif in proteins that typically consists of at least six histidine (His) residues, often at the N- or C-terminus of the protein. It is also known as a hexa histidine-tag, 6xHis-tag, or His6 tag.

  9. Histidinol dehydrogenase - Wikipedia

    en.wikipedia.org/wiki/Histidinol_dehydrogenase

    In enzymology, histidinol dehydrogenase (HIS4) (HDH) (EC 1.1.1.23) is an enzyme that catalyzes the chemical reaction. L-histidinol + 2 NAD + L-histidine + 2 NADH + 2 H +. Thus, the two substrates of this enzyme are L-histidinol and NAD +, whereas its 3 products are L-histidine, NADH, and H +.