Ferric Stability Constants of Representative Marine Siderophores: Marinobactins, Aquachelins, and Petrobactin

Zhang, Guangping; Amin, Shady A.; Küpper, Frithjof C.; Holt, Pamela D.; Carrano, Carl J.; Butler, Alison

doi:10.1021/ic901739m

Cited by 43 publications

(40 citation statements)

References 48 publications

(111 reference statements)

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“…They are named aerobactin if R 1 = R 2 = R = H; nannochelin C if R = -CHCHC 6 H 5 , R 1 = R 2 = H; nannochelin A if R 1 = R 2 = CH 3 and nannochelin B if R 1 = H, R 2 = CH 3 . Similar structure have various petrabactins, but with a longer chain including more amino groups and different final complex R segments, in the form of differently substituted 2,3-dihydroxybenzenes [579,583,589,594,596,601]. There is also a number of amino analogs of citric acid siderophores [572].…”

Section: Formation Of Amides Citrate-based Siderophores and Other Commentioning

confidence: 99%

Citric Acid

Apelblat¹

2014

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Section: Formation Of Amides Citrate-based Siderophores and Other Commentioning

confidence: 99%

Citric Acid

Apelblat¹

2014

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“…To calculate the proton independent formation constant, it is necessary to correct the free ligand concentration to that of the fully deprotonated form using the appropriate  function, calculated from the protonation constants of the ligand. 31,36,37 Using the four required protonation constants, log values of the overall proton independent stability constants were determined to be 34.4(4) for lystabactin A (1) and 35.8(7) for lystabactin B (2). Using these parameters, the pFe of lystabactin A (1) and lystabactin B (2) have been calculated to be 26.0 and 27.5, respectively.…”

Section: Iron Binding Properties Of Lystabactin a (1) And B (2)mentioning

confidence: 99%

Isolation, Structure Elucidation, and Iron-Binding Properties of Lystabactins, Siderophores Isolated from a Marine Pseudoalteromonas sp.

Zane

Butler

2013

J. Nat. Prod.

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The marine bacterium Pseudoalteromonas sp. S2B, isolated from the Gulf of Mexico after the Deepwater Horizon oil spill, was found to produce lystabactins A, B, and C (1−3), three new siderophores. The structures were elucidated through mass spectrometry, amino acid analysis, and NMR. The lystabactins are composed of serine (Ser), asparagine (Asn), two formylated/hydroxylated ornithines (FOHOrn), dihydroxy benzoic acid (Dhb), and a very unusual nonproteinogenic amino acid, 4,8-diamino-3-hydroxyoctanoic acid (LySta). The iron-binding properties of the compounds were investigated through a spectrophotometric competition.

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“…For example, 2,3-dihydroxybenzoate (diOH-Bz, often denoted Dhb, which may result in confusion with another monomer, dehydrobutyrin, present in ribosomal bacteriocins like nisin or subtilin [19]), found in enterobactin or bacillibactin (1), or the chromophore of pyoverdins (ChrP, a dihydroxyquinoline group which results from the condensation and subsequent modification of diaminobutyric acid, tyrosine, and a dicarboxylic acid or its monoamide [7]) contains a catecholate group. N-Formyl-N-OH-ornithine (Fo-OH-Orn), found in ornibactins (61), N-acetyl-N-OH-ornithine (Ac-OH-Orn), found in aquachelins (69), N-OH-cyclo-ornithine (OH-cOrn), found in pseudobactins (65), OH-histidine (OH-His), found in corrugatin (50), and OH-lysine (OH-Lys), found in mycobactins (59) all contain an hydroxamate group. OH-aspartate (OH-Asp) of the azotobactin D (13) contains a hydroxycarboxylate group.…”

Section: Study Of Biological Activity (I) Statistical Resultsmentioning

confidence: 99%

Diversity of Monomers in Nonribosomal Peptides: towards the Prediction of Origin and Biological Activity

et al. 2010

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Nonribosomal peptides (NRPs) are molecules produced by microorganisms that have a broad spectrum of biological activities and pharmaceutical applications (e.g., antibiotic, immunomodulating, and antitumor activities). One particularity of the NRPs is the biodiversity of their monomers, extending far beyond the 20 proteogenic amino acid residues. Norine, a comprehensive database of NRPs, allowed us to review for the first time the main characteristics of the NRPs and especially their monomer biodiversity. Our analysis highlighted a significant similarity relationship between NRPs synthesized by bacteria and those isolated from metazoa, especially from sponges, supporting the hypothesis that some NRPs isolated from sponges are actually synthesized by symbiotic bacteria rather than by the sponges themselves. A comparison of peptide monomeric compositions as a function of biological activity showed that some monomers are specific to a class of activities. An analysis of the monomer compositions of peptide products predicted from genomic information (metagenomics and high-throughput genome sequencing) or of new peptides detected by mass spectrometry analysis applied to a culture supernatant can provide indications of the origin of a peptide and/or its biological activity.Nonribosomal peptides (NRPs) are molecules produced by microorganisms and synthesized by huge multienzymatic complexes (38, 41), called nonribosomal peptide synthetases (NRPSs). These megaenzymes are organized into modules, one for each amino acid to be built into the peptide product. This is accomplished by division of each catalytic step into specialized semiautonomous domains. The basic set of domains (adenylation, thiolation, and condensation) within a module can be extended by substrate-modifying domains, including domains for substrate epimerization, ␤ hydroxylation, N methylation, and heterocyclic ring formation. The peptide release is catalyzed by a thioesterase domain which can also, in many cases, be involved in an intramolecular reaction leading to a cyclic or partially cyclic peptide or, in fewer cases, in the oligomerization of peptide units (iterative biosynthesis). NRPs show a broad spectrum of biological activities and pharmaceutical applications. They can harbor antimicrobial, immunomodulator, or antitumor activities. Cyclosporine (5), an immunosuppressant drug widely used in organ transplantation, daptomycin (60) (marketed in the United States under the trade name Cubicin), used in the treatment of certain infections caused by Gram-positive bacteria, aminoadipyl-cysteinylvaline (ACV)-tripeptide, which is the precursor of cephalosporin and penicillin (29), the most famous antibiotic, and also bleomycin (57), used in the treatment of several cancers, are some common examples of NRPs of high therapeutic importance. Two main structural traits distinguish these peptides from ribosomally synthesized peptides: first, their primary structure is more frequently cyclic (partially or totally) branched or polycyclic rather than linear and, seco...

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Ferric Stability Constants of Representative Marine Siderophores: Marinobactins, Aquachelins, and Petrobactin

Abstract: The coordination of iron(III) to the marine amphiphilic marinobactin and aquachelin siderophores, as well as to petrobactin, the unusual 3,4-dihydroxybenzoyl siderophore is reported. Potentiometric titrations were performed on the apo siderophore to determine the ligand pK a values,

Cited by 43 publications

References 48 publications

Citric Acid

Citric Acid

Isolation, Structure Elucidation, and Iron-Binding Properties of Lystabactins, Siderophores Isolated from a Marine Pseudoalteromonas sp.

Diversity of Monomers in Nonribosomal Peptides: towards the Prediction of Origin and Biological Activity

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