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In the oxygen-rich capillaries of the lung, this property causes the displacement of carbon dioxide to plasma as low-oxygen blood enters the alveolus and is vital for alveolar gas exchange. The general equation for the Haldane Effect is: H + + HbO 2 ⇌ H + Hb + O 2; However, this equation is confusing as it reflects primarily the Bohr effect.
Aerobic respiration requires oxygen (O 2) in order to create ATP.Although carbohydrates, fats and proteins are consumed as reactants, aerobic respiration is the preferred method of pyruvate production in glycolysis, and requires pyruvate to the mitochondria in order to be oxidized by the citric acid cycle.
Even though carbon dioxide is carried by hemoglobin, it does not compete with oxygen for the iron-binding positions but is bound to the amine groups of the protein chains attached to the heme groups. The iron ion may be either in the ferrous Fe 2+ or in the ferric Fe 3+ state, but ferrihemoglobin ( methemoglobin ) (Fe 3+ ) cannot bind oxygen ...
The naked mole rat has the unique ability to survive low oxygen conditions for no less than several hours, and zero oxygen conditions for 18 minutes. [100] One of the ways of combatting hypoxia in the brain is decreasing the reliance on oxygen for ATP production, achieved by decreased respiration rates and proton leak.
Although acids such as phosphoric acid are written as H 3 PO 4, the protons are attached to oxygen atoms forming hydroxyl groups, so the formula can also be written as OP(OH) 3 to better reflect the structure. Sulfuric acid may be written as O 2 S(OH) 2; this is the molecule observed in the gas phase.
Such complexes can be generated by treating low-valent metal complexes with oxygen. For example, Vaska's complex reversibly binds O 2 (Ph = C 6 H 5): IrCl(CO)(PPh 3) 2 + O 2 ⇌ IrCl(CO)(PPh 3) 2 O 2. The conversion is described as a 2 e − redox process: Ir(I) converts to Ir(III) as dioxygen converts to peroxide.
When deoxyhemoglobin picks up an oxygen molecule, this histidine residue moves away and returns once the oxygen is securely attached to form a hydrogen bond with it. This results in the Fe 2+ ion switching to a low-spin configuration, resulting in a 20% decrease in ionic radius so that now it can fit into the porphyrin ring, which becomes ...
The oxygen binding site is a binuclear iron center. The iron atoms are coordinated to the protein through the carboxylate side chains of a glutamate and aspartate and five histidine residues. The uptake of O 2 by hemerythrin is accompanied by two-electron oxidation of the reduced binuclear center to produce bound peroxide (OOH − ).