Where is oxygen attached on a hemoglobin molecule?
singleAnswer
iron ion iron atom
Hemoglobin
Where is oxygen attached on a hemoglobin molecule?
Hemoglobin Carboxyhemoglobin Carbaminohemoglobin Glycated hemoglobin Heme Structural Biochemistry/Protein function/Heme group/Hemoglobin ... Hemoglobin A Conjugated protein Globin 2,3-Bisphosphoglyceric acid
Hemoglobin (American English) or haemoglobin (British English) abbreviated Hb 
or Hgb, is the ... The mammalian <b>hemoglobin molecule</b> can bind (carry) up to four 
<b>oxygen</b> molecules. Hemoglobin is ... Excessive glucose in one&#39;s blood can <b>attach</b> 
to hemoglobin and raise the level of hemoglobin A1c. Hemoglobin and&nbsp;... Carboxyhemoglobin or carboxyhaemoglobin (symbol COHb or HbCO) is a stable 
complex of ... Carbon monoxide binds to hemoglobin at the same sites as <b>oxygen</b>
, but ... The slow release rate of carbon monoxide causes an accumulation of CO-
bound <b>hemoglobin molecules</b> as exposure to carbon monoxide continues. Carbaminohaemoglobin is a compound of hemoglobin and carbon dioxide, and 
is one of the ... In the absence of <b>oxygen</b>, unbound <b>hemoglobin molecules</b> have a 
greater chance of becoming carbaminohaemoglobin. The Haldane effect&nbsp;... Glycated hemoglobin is a form of hemoglobin (abbreviated Hb) that is chemically 
linked to a ... The process by which sugars <b>attach</b> to Hb is called glycation. HbA1c 
is a ... Once a <b>hemoglobin molecule</b> is glycated, it remains that way. A buildup&nbsp;... Heme (American English) or haem (British English) is a coordination complex &quot;
consisting of an ... In peroxidase reactions, the porphyrin <b>molecule</b> also serves as 
an electron source. ... This phenomenon, which states that <b>hemoglobin&#39;s oxygen</b> 
binding affinity is inversely proportional to both acidity and concentration of 
carbon&nbsp;... The fact that 2,3-BPG helps <b>hemoglobin</b> protein binding <b>oxygen molecule</b> for 
more <b>oxygen</b> to be delivered to body tissues is known as heterotropic allosteric&nbsp;... <b>Hemoglobin</b> A (HbA), also known as adult <b>hemoglobin</b>, <b>hemoglobin</b> A1 or α2β2, 
is the most common human <b>hemoglobin</b> tetramer, accounting for over 97% of the 
total red blood cell <b>hemoglobin</b>. <b>Hemoglobin</b> is an <b>oxygen</b>-binding protein, found 
in erythrocytes, which ... Each subunit contains a heme group that diatomic 
<b>oxygen</b> (O2) <b>molecules</b>&nbsp;... A conjugated protein is a protein that functions in interaction with other (non-
polypeptide) chemical groups <b>attached</b> by covalent bonding ... a co-ordinate 
bond with an <b>oxygen molecule</b> (O2), allowing <b>hemoglobin</b> to transport <b>oxygen</b> 
through&nbsp;... The globins are a superfamily of heme-containing globular proteins, involved in 
binding and/or transporting <b>oxygen</b>. These proteins all incorporate the globin fold
, a series of eight alpha helical segments. Two prominent members include 
myoglobin and <b>hemoglobin</b>. ... HbN (or GlbN): a truncated <b>haemoglobin</b>-like 
protein that binds <b>oxygen</b>&nbsp;... 2,3-Bisphosphoglyceric acid (conjugate base 2,3-bisphosphoglycerate) (2,3-BPG
), also known ... It fits neatly into the cavity of the deoxy- conformation, exploiting 
the <b>molecular</b> symmetry and positive polarity by forming salt bridges with lysine ... 
The accumulation of 2,3-BPG decreases the affinity of <b>hemoglobin</b> for <b>oxygen</b>.
The iron ion
Hemoglobin