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The pair in which both species have iron is (a) nitrogenase, cytochromes (b) carboxypeptidase, haemoglobin (c) haemocyanin, nitrogenase (d) haemoglobin cytochromes

Short Answer

Expert verified
Options (a) and (d) are correct, as both pairs contain iron.

Step by step solution

01

Understanding the Problem

We need to identify a pair of biological molecules, referred to as 'species', in which both members contain iron. The options provided are different pairs of biological molecules.
02

Analyze Each Option

Let's break down each option to check for iron presence: 1. **Nitrogenase**: Contains iron; it's an iron-sulfur enzyme. **Cytochromes**: Contain iron; they are heme proteins. 2. **Carboxypeptidase**: Contains zinc, not iron. **Haemoglobin**: Contains iron; it has an iron-containing heme group. 3. **Haemocyanin**: Contains copper, not iron. **Nitrogenase**: Contains iron. 4. **Haemoglobin**: Contains iron. **Cytochromes**: Contain iron.
03

Identify Correct Pair

From our analysis: - Option (a) Both nitrogenase and cytochromes contain iron. - Option (b) Carboxypeptidase does not contain iron. - Option (c) Haemocyanin does not contain iron. - Option (d) Both haemoglobin and cytochromes contain iron. Options (a) and (d) both consist of pairs that have iron.
04

Select the Correct Answers

Based on the analysis, the pairs that contain iron in both species are: - Option (a) nitrogenase, cytochromes - Option (d) haemoglobin, cytochromes

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Key Concepts

These are the key concepts you need to understand to accurately answer the question.

Iron-containing enzymes
Iron-containing enzymes play crucial roles in a range of biological systems. They act as catalysts, speeding up chemical reactions in cells. A good example is nitrogenase, an enzyme that facilitates the conversion of nitrogen gas from the atmosphere into ammonia. Iron is present in nitrogenase as part of an iron-sulfur cluster, which is essential for its activity. Another common class of iron-containing enzymes is cytochromes, which are involved in electron transport chains. These are vital in cellular respiration, helping cells to produce energy efficiently. Without iron, these enzymes would not function effectively, hindering biological processes necessary for life. This makes iron a critical element in enzyme function.
Heme proteins
Heme proteins are a group of proteins that contain an iron atom embedded in a heme group. The heme group is a complex ring-like structure that helps the protein in carrying out its functions. A familiar example of a heme protein is hemoglobin, which transports oxygen in the blood. The iron in the heme group binds to oxygen molecules, allowing hemoglobin to carry them through the bloodstream to cells. Another example is the cytochrome proteins found in the mitochondria. They play a key role in the process of energy production within cells through the electron transport chain. The presence of iron within the heme group is what allows these proteins to bind with gases like oxygen or transfer electrons, which is fundamental to their function.
Iron-sulfur clusters
Iron-sulfur clusters are assemblies of iron and sulfur atoms found in a wide variety of enzymes. These clusters are fundamental in facilitating electron transfers because they can easily gain and lose electrons. They are integral to enzymes like nitrogenase and play essential roles in metabolic pathways. The structure typically involves iron atoms coordinated with sulfur from cysteine amino acids in proteins. This arrangement provides stability and enables efficient electron transfer. Iron-sulfur clusters are also used in enzymes associated with DNA repair, energy production, and biosynthesis processes, showcasing their versatility and importance within biological systems.
Biological molecules with metal ions
Inorganic metal ions are found in various biological molecules and are crucial for the molecules' stability and function. These metal ions, such as iron, zinc, or copper, often act as cofactors, assisting in biochemical reactions. For instance, the enzyme carboxypeptidase contains zinc which is essential for its role in protein digestion. In contrast, hemoglobin relies on iron to carry oxygen. Each metal ion has unique properties that enable these biological molecules to perform specific functions. Through the selective incorporation of metal ions, organisms can conduct numerous biochemical processes, which underscores the significance of metal ions in maintaining life. Understanding these roles provides insight into how complex and efficient biological systems can be.

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Most popular questions from this chapter

Amongst the following, the lowest degree of paramagnetism per mole of the compound at \(298 \mathrm{~K}\) will be shown by (a) \(\mathrm{MnSO}_{4} \cdot 4 \mathrm{H}_{2} \mathrm{O}\) (b) \(\mathrm{CuSO}_{4} \cdot 5 \mathrm{H}_{2} \mathrm{O}\) (c) \(\mathrm{FeSO}_{4} \cdot 6 \mathrm{H}_{2} \mathrm{O}\) (d) \(\mathrm{NiSO}_{4} \cdot 6 \mathrm{H}_{2} \mathrm{O}\)

The pair of which salts is expected to have the same colour in their freshly prepared aqueous solutions. (a) \(\mathrm{VOCl}_{2}, \mathrm{CuCl}_{2}\) (b) \(\mathrm{CuCl}_{2}, \mathrm{FeCl}_{2}\) (c) \(\mathrm{FeCl}_{2}, \mathrm{VOCl}_{2}\) (d) \(\mathrm{MnCl}_{2}, \mathrm{FeCl}_{2}\)

Cerium \((\mathrm{Z}=58)\) is an important member of the lanthanoids. Which of the following statements about cerium is incorrect? (a) the common oxidation states of cerium are \(+3\) and \(+4\) (b) the \(+3\) oxidation state of cerium is more stable than the \(+4\) oxidation state (c) the \(+4\) oxidation state of cerium is not known in solutions (d) cerium (IV) acts as an oxidizing agent

The transition elements with some exceptions can show a large number of oxidation states. The various oxidation states are related to the electronic configuration of their atoms. The variable oxidation states of a transition metal is due to the involvement of \((\mathrm{n}-1) \mathrm{d}\) and outer \(\mathrm{ns}\)-electrons. For the first five elements of 3 d-transition series. The minimum oxidation state is equal to the number of electrons in 4s shell and the maximum oxidation state is equal to the sum of \(4 \mathrm{~s}\) and \(3 \mathrm{~d}\)-electrons. The relative stability of various oxidation state of a given element can be explained on the basis of stability of \(\mathrm{d}^{0}, \mathrm{~d}^{5}\) and \(\mathrm{d}^{10}\) configurations. Identify the correct statement (a) \(\mathrm{Ti}^{4+}, \mathrm{Mn}^{2+}\) are stable oxidation states (b) The most common oxidation state of 3 d-series is \(+2\) (c) The lowest oxidation state of \(\mathrm{Cr}\) and \(\mathrm{Cu}\) is \(+1\) while for others it is \(+2\). (d) All of these

The transition elements with some exceptions can show a large number of oxidation states. The various oxidation states are related to the electronic configuration of their atoms. The variable oxidation states of a transition metal is due to the involvement of \((\mathrm{n}-1) \mathrm{d}\) and outer \(\mathrm{ns}\)-electrons. For the first five elements of 3 d-transition series. The minimum oxidation state is equal to the number of electrons in 4s shell and the maximum oxidation state is equal to the sum of \(4 \mathrm{~s}\) and \(3 \mathrm{~d}\)-electrons. The relative stability of various oxidation state of a given element can be explained on the basis of stability of \(\mathrm{d}^{0}, \mathrm{~d}^{5}\) and \(\mathrm{d}^{10}\) configurations. In 3 d-series, the maximum oxidation state is shown by (a) \(\mathrm{Fe}(26)\) (b) Mn (atomic no.: 25 ) (c) \(\mathrm{Cr}(24)\) (d) Sc (atomic no: 21 )

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