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The chain of redox reactions driving the flow of electrons through the electron transport chain, from electron donors such as NADH to electron acceptors such as oxygen and hydrogen (protons), is an exergonic process – it releases energy, whereas the synthesis of ATP is an endergonic process, which requires an input of energy.
A sixth position can reversibly bind oxygen by a coordinate covalent bond, [48] completing the octahedral group of six ligands. This reversible bonding with oxygen is why hemoglobin is so useful for transporting oxygen around the body. [49] Oxygen binds in an "end-on bent" geometry where one oxygen atom binds to Fe and the other protrudes at an ...
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.
Phosphorylation is essential to the processes of both anaerobic and aerobic respiration, which involve the production of adenosine triphosphate (ATP), the "high-energy" exchange medium in the cell. During aerobic respiration, ATP is synthesized in the mitochondrion by addition of a third phosphate group to adenosine diphosphate (ADP) in a ...
Both feature a ring of many small alpha-helical proteins that rotate relative to nearby stationary proteins, using a H + potential gradient as an energy source. This link is tenuous, however, as the overall structure of flagellar motors is far more complex than that of the F O particle and the ring with about 30 rotating proteins is far larger ...
Cyanide, azide, and carbon monoxide [20] all bind to cytochrome c oxidase, inhibiting the protein from functioning and leading to the chemical asphyxiation of cells. Higher concentrations of molecular oxygen are needed to compensate for increasing inhibitor concentrations, leading to an overall decrease in metabolic activity in the cell in the ...
Most hemocyanins bind with oxygen non-cooperatively and are roughly one-fourth as efficient as hemoglobin at transporting oxygen per amount of blood. Hemoglobin binds oxygen cooperatively due to steric conformation changes in the protein complex , which increases hemoglobin's affinity for oxygen when partially oxygenated.
Like hemoglobin, myoglobin is a cytoplasmic protein that binds oxygen on a heme group. It harbors only one globulin group, whereas hemoglobin has four. Although its heme group is identical to those in Hb, Mb has a higher affinity for oxygen than does hemoglobin but fewer total oxygen-storage capacities. [22]