1g of Hb can bind with 1.34mL of oxygen instead 1.39 at full saturation because it does so at normal oxygen capacity.
paste, bind
C2a
Hydrogen
Dentisity is the number of atoms in a ligand that bond to cetral atom e.g. EN has 2 atoms that bind and cooordination number is the number of ligand atoms that bind to a center so for [K(en)3]3+ it is 6
bound, bind, contain, check, surround, restrain, inhibit, enclose, impede, handicap, diminish
It is not the fourth one specifically that binds easier, O2 is a positive allosteric effector (activator) of Haemoglobin and the binding of O2 facilitates further binding of O2. I'm not sure why this is though.
The molecule that can bind to RuBisCO and inhibit carbon fixation rates is oxygen. This process is known as photorespiration, and occurs when RuBisCO binds with oxygen instead of carbon dioxide, leading to a decrease in the efficiency of photosynthesis.
Nitrogen does not bind to hemoglobin in the way that oxygen does. Hemoglobin specifically binds to oxygen molecules for transport in the bloodstream. While nitrogen is present in the air we breathe, it is mostly inert and does not participate in the same biochemical interactions as oxygen with hemoglobin. Instead, nitrogen is dissolved in the blood but does not play a role in oxygen transport or exchange.
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.
One gram of hemoglobin can bind with approximately 1.34 milliliters of oxygen.
Mostly 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.
Carbon monoxide and oxygen.
Rubisco will only fix oxygen when carbon dioxide is in short supply or inaccessible (most commonly because of closed or partially closed stomata). When rubisco fixes oxygen instead of carbon, it is called photorespiration. This process probably evolved as an adaption to hot dry environments with limited amounts of carbon dioxide; however, photorespiration is a highly inefficient process.
The problem with carbon monoxide is that haemoglobin would much rather take it up than oxygen. In fact, haemoglobin has a 500 times greater affinity for carbon monoxide than with oxygen. Without oxygen being transported to our cells, respiration ceases and basic metabolic reactions in our body stop, and we quickly die from carbon monoxide poisoning.
The cooperativity of hemoglobin refers to how its binding of one oxygen molecule affects its ability to bind more oxygen molecules. When one oxygen molecule binds to hemoglobin, it changes the shape of the protein, making it easier for more oxygen molecules to bind. This makes hemoglobin more efficient at picking up oxygen in the lungs and releasing it to tissues that need it.
When hydrogen and oxygen bind to form water, the electrons are shared between the hydrogen and oxygen atoms. This sharing creates a stable covalent bond in the water molecule.