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Question

The correct statement(s) about enterobactin (ent) is(are)

Enterobactin Properties Explained

Enterobactin is a significant siderophore produced by many bacteria to scavenge iron ($Fe^{3+}$) from the environment. Understanding its structural components and iron-binding capabilities is crucial.

Correct Statements Analysis

  • Statement 1: It has three catechol moieties. Enterobactin's structure is characterized by three 2,3-dihydroxybenzoyl groups, commonly known as catechol moieties. These phenolic hydroxyl groups are primarily responsible for chelating the $Fe^{3+}$ ion due to their high affinity and ability to deprotonate.
  • Statement 2: It has a serine-trilactone backbone. Enterobactin is synthesized from the amino acid L-serine. During its formation, three serine residues undergo cyclization to form a central trilactone ring, which serves as the core scaffold connecting the catechol-containing side chains.
  • Statement 3: It binds with $Fe^{3+}$ ion to form $[Fe(ent)]^{3-}$ ion. Enterobactin acts as a hexadentate ligand, coordinating with one $Fe^{3+}$ ion using the oxygen atoms from its three catechol groups and three hydroxamate groups (derived from serine). The binding results in a stable complex. The formula $[Fe(ent)]^{3-}$ indicates that the enterobactin ligand carries a net charge of 3- within the complex, typically due to the deprotonation of the hydroxamate functional groups upon coordination with the ferric ion.

The primary iron-chelating groups in enterobactin are its catechol moieties and the deprotonated hydroxamate groups. Statement 4, mentioning only hydroxamic acid groups without the context of catechols or their role in the complex, is less precise compared to the other correct statements, especially considering the structure-function relationship emphasized in correct options 1 and 3.

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Important Questions from Bioinorganic Chemistry

  1. Consider the following transformation reactions in the context of co - enzyme B12

    A. 1, 2 - Carbon shift

    B. Hydration of CO2

    C. Benzene to phenol

    D. Dimethyl sulfide to dimethyl sulfoxide

    The correct statement(s) for co - enzyme B12 is / are

  2. During the binding of O2 to myoglobin (consider 'heme' in xy-plane), the molecular orbital of O2 and atomic orbital of Fe involved in the formation of the σ-bond is

  3. In the catalytic cycle of Cytochrome P450, the generation of [(porphyrin)+•FeIV(O)] from [(porphyrin)FeIII(OOH)] involves

  4. Match List I with List II

    List I

    List II

    Metalloprotein

    Metal

    A.

    carboxypeptidase A

    I.

    Mn

    B.

    oxygen-evolving complex

    II.

    Fe

    C.

    hemerythrin

    III.

    Ni

    D.

    coenzyme F-430

    IV.

    Zn

    Choose the correct answer from the options given below:

  5. In solution, Vaska's complex is known to bind O2 reversibly. In the product, oxidation state of the metal ion center coordination geometry and mode of binding of O2, respectively are

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