This article may be too technical for most readers to understand.(May 2023) |
Names | |
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Preferred IUPAC name 4-[4-[3-[(3,4-dihydroxybenzoyl)amino]propylamino]butylamino]-2-[2-[4-[3-[(3,4-dihydroxybenzoyl)amino]propylamino]butylamino]-2-oxoethyl]-2-hydroxy-4-oxobutanoic acid | |
Identifiers | |
3D model (JSmol) | |
ChEBI |
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ChemSpider | |
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PubChem CID | |
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Properties | |
C34H50N6O11 | |
Molar mass | 718.79 g·mol−1 |
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). |
Petrobactin is a bis-catechol siderophore found in M. hydrocarbonoclasticus, A. macleodii, and the anthrax-producing B. anthracis. [1] Like other siderophores petrobactin is a highly specific iron(III) transport ligand, contributing to the marine microbial uptake of environmental iron. [1] [2]
The iron-chelated petrobactin complex readily undergoes a photolytic oxidative decarboxylation due to its α-hydroxy carboxylate group, converting iron(III) to the more biologically useful iron(II). [3]
Like other siderophores, petrobactin is secreted by an animal pathogenic bacterium. B. anthracis uses petrobactin to acquire iron from its host. Interestingly, while the 3,4-catecholate ends of petrobactin do not improve iron(III) affinity relative to hydroxamate ends, they speed up iron removal from human diferric transferrin. [4] Petrobactin in its ferric and iron-free forms is bound selectively by YclQ (an isogenic disruption mutant in the transporter encoded by the yclNOPQ operon in Bacillus subtilis), as is petrobactin's precursor protocatechuic acid and the ferric petrobactin photoproduct. The yclNOPQ operon is required for the utlization of petrobactin and yclNOPQ orthologs likely contribute to the pathogenicity of Bacilli. [5]
In B. anthracis, petrobactin is produced by a nonribosomal peptide synthetase independent siderophore (NIS) synthetase pathway. [6] The enzyme sequences used are anthrax sidereophore biosynthesis (Asb) A through F, in alphabetical order. These gene clusters are identical to those used in M. hydrocarbonclasticus biosynthesis of petrobactin. In A. macleodii only the first three gene clusters, AsbA through AsbC, are identical to B. anthracis; then a longer AsbD and AsbF is next, followed by two hypothetical protein domains and a PepSY domain-containing gene. A. macleodii ends its sequence with AsbE. [1]
The biosynthesis of petrobactin in B. anthracis can progress in order AsbA-AsbB-AsbE-AsbE or AsbA-AsbE-AsbB-AsbE. [7]
If the enzymation reactions in this pathway proceed generally, in domains AsbA and AsbB the phosphorylation of a carboxylic acid forms an acylphosphate intermediate, which is then dephosphorylated by a primary amine in spermidine. In domain AsbE the lone pair of electrons on a primary amine allows for a nucleophilic attack on the electrophilic hydroxyl carbon. The sulfur on AsbE is protonated to form a thiol and the amide nitrogen is deprotonated. [8]
The dehydration of 3-dehydroshikimic acid might proceed as a modified, enzyme-catalyzed dienol benzene rearrangement and reduction, leading to aromatization of the ring. [9]
Siderophores (Greek: "iron carrier") are small, high-affinity iron-chelating compounds that are secreted by microorganisms such as bacteria and fungi. They help the organism accumulate iron. Although a widening range of siderophore functions is now being appreciated, siderophores are among the strongest (highest affinity) Fe3+ binding agents known. Phytosiderophores are siderophores produced by plants.
Nonribosomal peptides (NRP) are a class of peptide secondary metabolites, usually produced by microorganisms like bacteria and fungi. Nonribosomal peptides are also found in higher organisms, such as nudibranchs, but are thought to be made by bacteria inside these organisms. While there exist a wide range of peptides that are not synthesized by ribosomes, the term nonribosomal peptide typically refers to a very specific set of these as discussed in this article.
Transition metal dinitrogen complexes are coordination compounds that contain transition metals as ion centers the dinitrogen molecules (N2) as ligands.
o-Succinylbenzoate—CoA ligase, encoded from the menE gene in Escherichia coli, catalyzes the fifth reaction in the synthesis of menaquinone. This pathway is called 1, 4-dihydroxy-2-naphthoate biosynthesis I. Vitamin K is a quinone that serves as an electron transporter during anaerobic respiration. This process of anaerobic respiration allows the bacteria to generate the energy required to survive.
Bacillus anthracis is a gram-positive and rod-shaped bacterium that causes anthrax, a deadly disease to livestock and, occasionally, to humans. It is the only permanent (obligate) pathogen within the genus Bacillus. Its infection is a type of zoonosis, as it is transmitted from animals to humans. It was discovered by a German physician Robert Koch in 1876, and became the first bacterium to be experimentally shown as a pathogen. The discovery was also the first scientific evidence for the germ theory of diseases.
Bacillithiol is a thiol compound found in Bacillus species. It is likely involved in maintaining cellular redox balance and plays a role in microbial resistance to the antibiotic fosfomycin.
Edward I. Solomon is the Monroe E. Spaght Professor of Chemistry at Stanford University. He is an elected member of the United States National Academy of Sciences, a Fellow of the American Association for the Advancement of Science, and a Fellow of the American Academy of Arts and Sciences. He has been profiled in the Proceedings of the National Academy of Sciences. He has also been a longtime collaborator with many scientists, including Professor Kenneth D. Karlin at Johns Hopkins University.
The Tsuji–Trost reaction is a palladium-catalysed substitution reaction involving a substrate that contains a leaving group in an allylic position. The palladium catalyst first coordinates with the allyl group and then undergoes oxidative addition, forming the π-allyl complex. This allyl complex can then be attacked by a nucleophile, resulting in the substituted product.
Yersiniabactin (Ybt) is a siderophore found in the pathogenic bacteria Yersinia pestis, Yersinia pseudotuberculosis, and Yersinia enterocolitica, as well as several strains of enterobacteria including enteropathogenic Escherichia coli and Salmonella enterica. Siderophores, compounds of low molecular mass with high affinities for ferric iron, are important virulence factors in pathogenic bacteria. Iron—an essential element for life used for such cellular processes as respiration and DNA replication—is extensively chelated by host proteins like lactoferrin and ferritin; thus, the pathogen produces molecules with an even higher affinity for Fe3+ than these proteins in order to acquire sufficient iron for growth. As a part of such an iron-uptake system, yersiniabactin plays an important role in pathogenicity of Y. pestis, Y. pseudotuberculosis, and Y. entercolitica.
Many bacteria secrete small iron-binding molecules called siderophores, which bind strongly to ferric ions. FepA is an integral bacterial outer membrane porin protein that belongs to outer membrane receptor family and provides the active transport of iron bound by the siderophore enterobactin from the extracellular space, into the periplasm of Gram-negative bacteria. FepA has also been shown to transport vitamin B12, and colicins B and D as well. This protein belongs to family of ligand-gated protein channels.
3-dehydroshikimate dehydratase (EC 4.2.1.118) is an enzyme with systematic name 3-dehydroshikimate hydro-lyase. This enzyme catalyses the following chemical reaction
Plantazolicin (PZN) is a natural antibiotic produced by the gram-positive soil bacterium Bacillus velezensis FZB42. PZN has specifically been identified as a selective bactericidal agent active against Bacillus anthracis, the causative agent of anthrax. This natural product is a ribosomally synthesized and post-translationally modified peptide (RiPP); it can be classified further as a thiazole/oxazole-modified microcin (TOMM) or a linear azole-containing peptide (LAP).
Bacillibactin is a catechol-based siderophore secreted by members of the genus Bacillus, including Bacillus anthracis and Bacillus subtilis. It is involved in the chelation of ferric iron (Fe3+) from the surrounding environment and is subsequently transferred into the bacterial cytoplasm via the use of ABC transporters.
Siderocalin(Scn), lipocalin-2, NGAL, 24p3 is a mammalian lipocalin-type protein that can prevent iron acquisition by pathogenic bacteria by binding siderophores, which are iron-binding chelators made by microorganisms. Iron serves as a key nutrient in host-pathogen interactions, and pathogens can acquire iron from the host organism via synthesis and release siderophores such as enterobactin. Siderocalin is a part of the mammalian defence mechanism and acts as an antibacterial agent. Crystallographic studies of Scn demonstrated that it includes a calyx, a ligand-binding domain that is lined with polar cationic groups. Central to the siderophore/siderocalin recognition mechanism are hybrid electrostatic/cation-pi interactions. To evade the host defences, pathogens evolved to produce structurally varied siderophores that would not be recognized by siderocalin, allowing the bacteria to acquire iron.
Rebecca Abergel is a French inorganic chemist who specializes in the coordination chemistry between lanthanide and actinide complexes. Alongside the effects of heavy element exposure and contamination on different biological systems. Abergel is currently a faculty scientist and heavy element chemistry group leader at the chemical sciences division of Lawrence Berkeley National Laboratory in Berkeley, California. She is also assistant professor of nuclear engineering at University of California, Berkeley.
Serena DeBeer is an American chemist. She is currently a W3-Professor and the director at the Max Planck Institute for Chemical Energy Conversion in Muelheim an der Ruhr, Germany, where she heads the Department of Inorganic Spectroscopy. Her expertise lies in the application and development of X-ray based spectroscopic methods as probes of electronic structure in biological and chemical catalysis.
Pyonitrins are a family of highly hydrogen-deficient alkaloids discovered from an insect-associated Pseudomonas protegens strain. In vivo, pyonitrins A-D show activity against pathogen Candida albicans, which commonly cause bloodstream infections.
Paula L. Diaconescu is a Romanian-American chemistry professor at the University of California, Los Angeles. She is known for her research on the synthesis of redox active transition metal complexes, the synthesis of lanthanide complexes, metal-induced small molecule activation, and polymerization reactions. She is a fellow of the American Association for the Advancement of Science.
Kenichi Yokoyama is an enzymologist, chemical biologist, and natural product biochemist originally from Tokyo, Japan. He is an Associate Professor of Biochemistry at Duke University School of Medicine. In 2019, Yokoyama was awarded the Pfizer Award in Enzyme Chemistry from the American Chemical Society.
Katherine Barbeau is a professor at Scripps Institution of Oceanography known for her work on trace metals and the linkages between trace metals and biology.