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  2. Apomyoglobin - Wikipedia

    en.wikipedia.org/wiki/Apomyoglobin

    Apomyoglobin is a type of myoglobin that does not have a haem group. [3] This means that apomyoglobin lacks the haem groups that would have their iron atoms bind to Oxygen. [ 4 ] There is a possibility, however, that apomyoglobin can bind to other different cofactors that is not a haem group. [ 5 ]

  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. Neuroglobin - Wikipedia

    en.wikipedia.org/wiki/Neuroglobin

    Neuroglobin is a member of the vertebrate globin family involved in cellular oxygen homeostasis and reactive oxygen/nitrogen scavenging. It is an intracellular hemoprotein expressed in the central and peripheral nervous system, cerebrospinal fluid, retina and endocrine tissues.

  5. Transition metal dioxygen complex - Wikipedia

    en.wikipedia.org/wiki/Transition_metal_dioxygen...

    Myoglobin and hemoglobin are famous examples, and many synthetic analogues have been described that behave similarly. Binding of O 2 is usually described as proceeding by electron transfer from the metal(II) center to give superoxide (O − 2) complexes of metal(III) centers.

  6. Hemoprotein - Wikipedia

    en.wikipedia.org/wiki/Hemoprotein

    Myoglobin and hemoglobin are globular proteins that serve to bind and deliver oxygen using a prosthetic group. These globins dramatically improve the concentration of molecular oxygen that can be carried in the biological fluids of vertebrates and some invertebrates. Differences occur in ligand binding and allosteric regulation.

  7. Oxygen–hemoglobin dissociation curve - Wikipedia

    en.wikipedia.org/wiki/Oxygen–hemoglobin...

    These molecules of oxygen bind to the globin chain of the heme prosthetic group. [1] When hemoglobin has no bound oxygen, nor bound carbon dioxide, it has the unbound conformation (shape). The binding of the first oxygen molecule induces change in the shape of the hemoglobin that increases its ability to bind to the other three oxygen molecules.

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