Answer: Complex IV, also known as cytochrome c oxidase, oxidizes cytochrome c and transfers the electrons to oxygen, the final electron carrier in aerobic cellular respiration. The cytochrome proteins a and a3, in addition to heme and copper groups in complex IV transfer the donated electrons to the bound dioxygen species, converting it into molecules of water. The free energy from the electron transfer causes 4 protons to move into the intermembrane space contributing to the proton gradient. Oxygen reduces via the following reaction:
2 cytochrome c(red) + ½O2 + 4 H+(matrix) -> 2 cytochrome c(ox) + 1 H2O + 2 H+(intermembrane)
Explanation:
In the electron transport chain (ETC), the electrons go through a chain of proteins that increases its reduction potential and causes a release in energy. Most of this energy is dissipated as heat or utilized to pump hydrogen ions (H+) from the mitochondrial matrix to the intermembrane space and create a proton gradient. This gradient increases the acidity in the intermembrane space and creates an electrical difference with a positive charge outside and a negative charge inside. The ETC proteins in a general order are complex I, complex II, coenzyme Q, complex III, cytochrome C, and complex IV.
Because different restriction sites are used by different restriction enzymes to cleave DNA.
<h3>What is restriction sites?</h3>
- A restriction site is a segment of DNA with a base pair count between 6 and 8 that binds to a certain restriction enzyme. There are numerous restriction enzymes that have been identified from bacteria. By cleaving the viral DNA, they naturally render invasive viruses inactive.
- Restriction enzymes are beneficial in a variety of contexts. Each organism has a unique DNA sequence, so each one will have a unique arrangement of restriction sites.
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The answer is D. Mutualism is the symbiotic relationship when both organisms benefit. Predation is not a symbiotic relationship. Parasitism is the symbiotic relationship where one organism benefits and the other is harmed.
