http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=349150
yes, all aerobic cells are oxidase positive. The oxidase test is testing for the presence of cytochrome oxidase [by reducing it with an artificial substrate which turns purple when oxidised]. In aerobic cells cytochrome oxidase's normal role is in the electron transport chain, passing electrons from cytochrome c to oxygen. hence if the cell is aerobic then oxygen is terminal electron acceptor in the cells ETC and thus it will give a positive result in the oxidase test.
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Cytochrome c is a protein present in all aerobic organisms, and its sequence is highly conserved across species. By comparing the amino acid sequences of cytochrome c among different organisms, scientists can infer evolutionary relationships. The similarities and differences in cytochrome c sequences provide evidence for common ancestry and the process of evolution.
Humans are more closely related to chimpanzees than garden snails.
The media for oxidase test is differential, not selective. It helps differentiate between bacteria that produce the enzyme cytochrome c oxidase (positive result) and those that do not (negative result).
the mineral is iron.
yes, all aerobic cells are oxidase positive. The oxidase test is testing for the presence of cytochrome oxidase [by reducing it with an artificial substrate which turns purple when oxidised]. In aerobic cells cytochrome oxidase's normal role is in the electron transport chain, passing electrons from cytochrome c to oxygen. hence if the cell is aerobic then oxygen is terminal electron acceptor in the cells ETC and thus it will give a positive result in the oxidase test.
Azide kills bacteria by inhibiting the activity of cytochrome c oxidase, a key enzyme involved in the electron transport chain of bacterial cells. This inhibition disrupts the production of ATP, which is essential for bacterial survival and growth.
Cytochrome c is a protein that is typically described as brown or brownish-red in color.
One can buy cytochrome c, a highly conserved model protein for molecular evolution. After supplied, the cytochrome c product stays stable for five years.
The great apes (such as chimpanzees and gorillas) have cytochrome c sequences that are most similar to human cytochrome c. They share a common ancestor with humans relatively recently in evolutionary terms, resulting in a high degree of sequence similarity.
Humans have only one cytochrome c gene, which encodes a single protein that is essential for the electron transport chain in mitochondria. This protein plays a crucial role in cellular respiration by transferring electrons between complexes in the chain.
An oxidase test relies on a reagent that will change colors when it is oxidized. The reagent used in the test only reacts to cytochrome c oxidase by acting in place of oxygen to receive electrons from the cytochrome.
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The sequence of electron carriers in the electron transport chain starting with the least electronegative includes NADH dehydrogenase, ubiquinone, cytochrome b-c1 complex, cytochrome c, and cytochrome oxidase. These carriers are responsible for transferring electrons, creating a proton gradient, and ultimately generating ATP through oxidative phosphorylation.
The relative differences in cytochrome c among various species suggest evolutionary relationships and divergence among those species. More closely related species tend to have more similar cytochrome c sequences, indicating a common ancestry. Conversely, significant differences in the cytochrome c protein sequences may point to a longer evolutionary distance and divergence from a common ancestor. This information can be useful for phylogenetic studies and understanding evolutionary processes.