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When deoxyhemoglobin binds to oxygen it becomes oxidized hemoglobin?
False
What is the difference between deoxyhemoglobin and oxyhemoglobin?
Deoxy no oxygen and is purple. Oxy is with oxygen and is bright red color
When hemoglobin is not bound to oxygen it appears blue?
When hemoglobin is not combined with oxygen, it appears dark red.
What is the color of deoxyhemoglobin?
Dark red, almost burgundy. But the vein that carries the RBC filled with deoxyhemolgobin looks bluish because of the venous tissue, not deoxyhemoglobin.
What color is deoxyhemoglobin?
Deoxyhemoglobin is a dark red or maroon color. It appears this way because it lacks oxygen, which gives it a more bluish or purplish hue when bound to hemoglobin.
What is the difference in color in oxyhemoglobin and deoxyhemoglobin?
Oxyhemoglobin is bright red in color, while deoxyhemoglobin is darker, more bluish-red in color. This difference is due to the presence of oxygen in oxyhemoglobin, which gives it its bright red color.
What is the difference between deoxyhemoglobin and reduced hemoglobin?
Reduced hemoglobin does not have the oxygen molecules that oxyhemoglobin has. :)
Why deoxyhemoglobin is blue colour?
Deoxyhemoglobin appears blue because it reflects more blue light due to the absence of oxygen bound to the iron in its structure. The iron in deoxyhemoglobin results in a different electronic structure that absorbs less red light and reflects more blue light, giving it a bluish color.
How many oxygen molecules bind to myoglobin?
1 Each myoglobin molecule has one heme group and can bind one oxygen molecule. Hemoglobin on the other hand can bind up to 4 molecules of oxygen.
How much oxygen does one gram of hemogloblin bind with?
One gram of hemoglobin can bind with approximately 1.34 milliliters of oxygen.
What does hemoglobin bind with?
Mostly oxygen.
How does the cooperativity effect in haemoglobin contribute to its ability to efficiently bind and release oxygen?
The cooperativity effect in hemoglobin allows it to efficiently bind and release oxygen by enabling one oxygen molecule to bind to one subunit of hemoglobin, which triggers a conformational change in the protein structure that makes it easier for other oxygen molecules to bind. This cooperative binding and release mechanism helps hemoglobin efficiently transport oxygen throughout the body.
