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  2. Hemoglobin - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin

    Hemoglobin can bind protons and carbon dioxide, which causes a conformational change in the protein and facilitates the release of oxygen. Protons bind at various places on the protein, while carbon dioxide binds at the α-amino group. [71] Carbon dioxide binds to hemoglobin and forms carbaminohemoglobin. [72]

  3. Hemoprotein - Wikipedia

    en.wikipedia.org/wiki/Hemoprotein

    It binds to the 6th coordination position of the iron, His-E7 of the myoglobin binds to the oxygen that is now covalently bonded to the iron. The same is true for hemoglobin; however, being a protein with four subunits, hemoglobin contains four heme units in total, allowing four oxygen molecules in total to bind to the protein.

  4. Oxidative phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Oxidative_phosphorylation

    The chain of redox reactions driving the flow of electrons through the electron transport chain, from electron donors such as NADH to electron acceptors such as oxygen and hydrogen (protons), is an exergonic process – it releases energy, whereas the synthesis of ATP is an endergonic process, which requires an input of energy.

  5. Heme - Wikipedia

    en.wikipedia.org/wiki/Heme

    Binding of oxygen to a heme prosthetic group. Heme (American English), or haem (Commonwealth English, both pronounced /hi:m/ HEEM), is a ring-shaped iron-containing molecular component of hemoglobin, which is necessary to bind oxygen in the bloodstream. It is composed of four pyrrole rings with 2 vinyl and 2 propionic acid side chains. [1]

  6. Carbaminohemoglobin - Wikipedia

    en.wikipedia.org/wiki/Carbaminohemoglobin

    Because the formation of this compound generates hydrogen ions, haemoglobin is needed to buffer it. [12] Hemoglobin can bind to four molecules of carbon dioxide. The carbon dioxide molecules form a carbamate with the four terminal-amine groups of the four protein chains in the deoxy form of the molecule. Thus, one hemoglobin molecule can ...

  7. Myoglobin - Wikipedia

    en.wikipedia.org/wiki/Myoglobin

    Like hemoglobin, myoglobin is a cytoplasmic protein that binds oxygen on a heme group. It harbors only one globulin group, whereas hemoglobin has four. Although its heme group is identical to those in Hb, Mb has a higher affinity for oxygen than does hemoglobin but fewer total oxygen-storage capacities. [22]

  8. Cellular respiration - Wikipedia

    en.wikipedia.org/wiki/Cellular_respiration

    Aerobic respiration requires oxygen (O 2) in order to create ATP.Although carbohydrates, fats and proteins are consumed as reactants, aerobic respiration is the preferred method of pyruvate production in glycolysis, and requires pyruvate to the mitochondria in order to be oxidized by the citric acid cycle.

  9. Hemocyanin - Wikipedia

    en.wikipedia.org/wiki/Hemocyanin

    Most hemocyanins bind with oxygen non-cooperatively and are roughly one-fourth as efficient as hemoglobin at transporting oxygen per amount of blood. Hemoglobin binds oxygen cooperatively due to steric conformation changes in the protein complex , which increases hemoglobin's affinity for oxygen when partially oxygenated.