Assertion: hemoglobin's oxygen | /r/HasProperty | bound
Facets:
Source sentences:
text: The iron atom in the heme group must initially be in the ferrous (Fe2+) oxidation state to support oxygen and other gases' binding and transport (it temporarily switches to ferric during the time oxygen is bound, as explained above).
text: When hemoglobin has no bound oxygen, nor bound carbon dioxide, it has the unbound conformation (shape).
text: Hemoglobin releases the bound oxygen when carbonic acid is present, as it is in the tissues.
text: When the next oxygen is bound, another conformational change occurs to further supplement binding;
text: The increased stability of the T-state results in a decreased affinity for oxygen, since normally it is the intense straining of the T-state that drives deoxyhemoglobin to bind to oxygen; once oxygen is bound, the T-state loses its strain and relaxes into the R-state.
text: The iron atom in the heme group must initially be in the ferrous (Fe2+) oxidation state to support oxygen and other gases' binding and transport (it temporarily switches to ferric during the time oxygen is bound, as explained above).
text: (Refer to the handout for a diagram of how subtle the change in heme conformation is when oxygen is bound.)
text: For horse and human hemoglobin, on the other hand, the enhancement of affinity goes up in a more nearly regular and progressive fashion for each oxygen that is bound; though here again the biggest change seems to come at the last step.)' Certainly the binding of oxygen to any one of the hemes sets up far- reaching repercussions elsewhere in the molecule; and these appear to be particularly great after three of the heme groups are occupied by oxygens.
text: The iron atom in the heme group must initially be in the ferrous (Fe2+) oxidation state to support oxygen and other gases' binding and transport (it temporarily switches to ferric during the time oxygen is bound, as explained above).