Oxygen Carriers Flashcards
(152 cards)
Assertion
Reason
Free haem in solution binds CO with extremely high affinity.
The linear Fe–C–O bond geometry is favored in free haem.
The side chains of glutamate and aspartate participate in the Bohr effect.
Their pKs lie between 7 and 8.
Histidine residues contribute to buffering capacity in haemoglobin.
Histidine has a pK around 6.5 and can bind/release H+.
Foetal haemoglobin binds 2,3-BPG tightly.
H143β is replaced with serine in foetal Hb, which repels BPG.
In the absence of 2,3-BPG, haemoglobin’s oxygen affinity is lower.
2,3-BPG lowers oxygen affinity of haemoglobin.
Free haem in solution binds CO with extremely high affinity.
The linear Fe–C–O bond geometry is favored in free haem.
The side chains of glutamate and aspartate participate in the Bohr effect.
Their pKs lie between 7 and 8.
Histidine residues contribute to buffering capacity in haemoglobin.
Histidine has a pK around 6.5 and can bind/release H+.
Foetal haemoglobin binds 2,3-BPG tightly.
H143β is replaced with serine in foetal Hb, which repels BPG.
In the absence of 2,3-BPG, haemoglobin’s oxygen affinity is lower.
2,3-BPG lowers oxygen affinity of haemoglobin.
Free haem in solution binds CO with extremely high affinity.
The linear Fe–C–O bond geometry is favored in free haem.
The side chains of glutamate and aspartate participate in the Bohr effect.
Their pKs lie between 7 and 8.
Histidine residues contribute to buffering capacity in haemoglobin.
Histidine has a pK around 6.5 and can bind/release H+.
Foetal haemoglobin binds 2,3-BPG tightly.
H143β is replaced with serine in foetal Hb, which repels BPG.
In the absence of 2,3-BPG, haemoglobin’s oxygen affinity is lower.
2,3-BPG lowers oxygen affinity of haemoglobin.
Free haem in solution binds CO with extremely high affinity.
The linear Fe–C–O bond geometry is favored in free haem.
The side chains of glutamate and aspartate participate in the Bohr effect.
Their pKs lie between 7 and 8.
Histidine residues contribute to buffering capacity in haemoglobin.
Histidine has a pK around 6.5 and can bind/release H+.
Foetal haemoglobin binds 2,3-BPG tightly.
H143β is replaced with serine in foetal Hb, which repels BPG.
In the absence of 2,3-BPG, haemoglobin’s oxygen affinity is lower.
2,3-BPG lowers oxygen affinity of haemoglobin.
Free haem in solution binds CO with extremely high affinity.
The linear Fe–C–O bond geometry is favored in free haem.
The side chains of glutamate and aspartate participate in the Bohr effect.
Their pKs lie between 7 and 8.
Histidine residues contribute to buffering capacity in haemoglobin.
Histidine has a pK around 6.5 and can bind/release H+.