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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. 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]

  4. 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]

  5. Oxidative phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Oxidative_phosphorylation

    The protein then closes up around the molecules and binds them loosely – the "loose" state (shown in red). The enzyme then changes shape again and forces these molecules together, with the active site in the resulting "tight" state (shown in pink) binding the newly produced ATP molecule with very high affinity .

  6. Globin - Wikipedia

    en.wikipedia.org/wiki/Globin

    The globins are a superfamily of heme-containing globular proteins, involved in binding and/or transporting oxygen. These proteins all incorporate the globin fold, a series of eight alpha helical segments. Two prominent members include myoglobin and hemoglobin. Both of these proteins reversibly bind oxygen via a heme prosthetic group.

  7. Hemocyanin - Wikipedia

    en.wikipedia.org/wiki/Hemocyanin

    Hemocyanin is made of many individual subunit proteins, each of which contains two copper atoms and can bind one oxygen molecule (O 2). Each subunit weighs about 75 kilodaltons (kDa). Subunits may be arranged in dimers or hexamers depending on species; the dimer or hexamer complex is likewise arranged in chains or clusters with weights ...

  8. 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.

  9. Cytochrome c oxidase - Wikipedia

    en.wikipedia.org/wiki/Cytochrome_c_oxidase

    Cyanide, azide, and carbon monoxide [20] all bind to cytochrome c oxidase, inhibiting the protein from functioning and leading to the chemical asphyxiation of cells. Higher concentrations of molecular oxygen are needed to compensate for increasing inhibitor concentrations, leading to an overall decrease in metabolic activity in the cell in the ...