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Ubiquinone (coenzyme Q) and cytochrome c are both essential components of the electron transport chain in cellular respiration. They function as electron carriers, facilitating the transfer of electrons between different complexes within the mitochondrial membrane. Additionally, both molecules play a crucial role in the production of adenosine triphosphate (ATP) by contributing to the proton gradient that drives ATP synthesis. Their cooperative action is vital for efficient energy production in aerobic organisms.

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What is the sequence of electron carriers in the electron transport chain starting with the least electronegative?

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.


What organism whose cytochrome c is most like human cytochrome c?

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.


What are the carrier proteins in the electron transport chain?

The carrier proteins in the electron transport chain include NADH dehydrogenase (Complex I), cytochrome b-c1 complex (Complex III), cytochrome c, cytochrome oxidase (Complex IV), and ubiquinone (coenzyme Q). These proteins facilitate the transfer of electrons from NADH and FADH2 to ultimately generate ATP through oxidative phosphorylation.


Cytochrome c is a protein found in the electron transport chain of all eukaryotes. The table below shows the relative differences in cytochrome c among several species. What conclusion can you draw fr?

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.


How is cytochrome c used biochemical evidence for evolution?

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.


How cytochrome c provides evidence of evolution?

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What is the colour of cytochrome c?

Cytochrome c is a protein that is typically described as brown or brownish-red in color.


What can one buy from the store Cytochrome?

One can buy cytochrome c, a highly conserved model protein for molecular evolution. After supplied, the cytochrome c product stays stable for five years.


How many cytochrome c do humans have?

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.


How does cytochrome c provide evidence of evolution?

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What are the component of ETC in order of increase in redox potential?

The components of the electron transport chain (ETC) in order of increasing redox potential are: NADH dehydrogenase (Complex I), succinate dehydrogenase (Complex II), coenzyme Q (ubiquinone), cytochrome b-c1 complex (Complex III), cytochrome c, and finally cytochrome oxidase (Complex IV). As electrons move through these complexes, they are transferred from lower to higher redox potentials, facilitating the production of ATP through oxidative phosphorylation. This gradual increase in redox potential allows for the efficient release of energy necessary for ATP synthesis.


What has the author J C Horton written?

J. C. Horton has written: 'Cytochrome oxidase patches'