Siderophores: From natural roles to potential applications

Albelda-Berenguer, Magdalena; Monachon, Mathilde; Joseph, Edith

doi:10.1016/bs.aambs.2018.12.001

Cited by 83 publications

(79 citation statements)

References 107 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…These hydroxamates are precursors in the biosynthesis of siderophores; low molecular-weight iron chelators, which are secreted to then be imported in their iron-loaded form [37]. Iron is involved in several pivotal cellular processes, such as oxygen transport, respiration, nitrogen fixation, photosynthesis, and synthesis of DNA, fatty acids, and amino acids [38,39].…”

Section: N-hydroxylating Monooxygenasesmentioning

confidence: 99%

“…NHMOs are of emerging interest due to their application in medicine, reprocessing of nuclear fuel, remediation of metal-contaminated sites and the treatment of industrial waste [38,40]. For example, a NHMO was recently characterized to N-hydroxylate aminopropylphosphonate, an intermediate step towards the production of phosphonic acid FR-900098 with potent anti-malaria activity [41].…”

Section: N-hydroxylating Monooxygenasesmentioning

confidence: 99%

See 1 more Smart Citation

The “Green” FMOs: Diversity, Functionality and Application of Plant Flavoproteins

Thodberg

Neilson

2020

Catalysts

View full text Add to dashboard Cite

Flavin-dependent monooxygenases (FMOs) are ancient enzymes present in all kingdoms of life. FMOs typically catalyze the incorporation of an oxygen atom from molecular oxygen into small molecules. To date, the majority of functional characterization studies have been performed on mammalian, fungal and bacterial FMOs, showing that they play fundamental roles in drug and xenobiotic metabolism. By contrast, our understanding of FMOs across the plant kingdom is very limited, despite plants possessing far greater FMO diversity compared to both bacteria and other multicellular organisms. Here, we review the progress of plant FMO research, with a focus on FMO diversity and functionality. Significantly, of the FMOs characterized to date, they all perform oxygenation reactions that are crucial steps within hormone metabolism, pathogen resistance, signaling and chemical defense. This demonstrates the fundamental role FMOs have within plant metabolism, and presents significant opportunities for future research pursuits and downstream applications.

show abstract

Section: N-hydroxylating Monooxygenasesmentioning

confidence: 99%

Section: N-hydroxylating Monooxygenasesmentioning

confidence: 99%

The “Green” FMOs: Diversity, Functionality and Application of Plant Flavoproteins

Thodberg

Neilson

2020

Catalysts

View full text Add to dashboard Cite

show abstract

“…The diverse nature of siderophores and their structural as well as functional elements provide access towards many applications, as has been extensively reviewed (Saha et al 2016;Su et al 2018;Albelda-Berenguer et al 2019;Řezanka et al 2019;Hofmann et al 2020) and will not be discussed in detail here. a b c Fig.…”

Section: Nmos Involved In Siderophore Biosynthesismentioning

confidence: 99%

Flavin-dependent N-hydroxylating enzymes: distribution and application

Mügge

Heine

Baraibar

et al. 2020

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

Amino groups derived from naturally abundant amino acids or (di)amines can be used as "shuttles" in nature for oxygen transfer to provide intermediates or products comprising NO functional groups such as N-hydroxy, oxazine, isoxazolidine, nitro, nitrone, oxime, C-, S-, or N-nitroso, and azoxy units. To this end, molecular oxygen is activated by flavin, heme, or metal cofactorcontaining enzymes and transferred to initially obtain N-hydroxy compounds, which can be further functionalized. In this review, we focus on flavin-dependent N-hydroxylating enzymes, which play a major role in the production of secondary metabolites, such as siderophores or antimicrobial agents. Flavoprotein monooxygenases of higher organisms (among others, in humans) can interact with nitrogen-bearing secondary metabolites or are relevant with respect to detoxification metabolism and are thus of importance to understand potential medical applications. Many enzymes that catalyze N-hydroxylation reactions have specific substrate scopes and others are rather relaxed. The subsequent conversion towards various NO or N-N comprising molecules is also described. Overall, flavin-dependent N-hydroxylating enzymes can accept amines, diamines, amino acids, amino sugars, and amino aromatic compounds and thus provide access to versatile families of compounds containing the NO motif. Natural roles as well as synthetic applications are highlighted. Key points • NO and N-N comprising natural and (semi)synthetic products are highlighted. • Flavin-based NMOs with respect to mechanism, structure, and phylogeny are reviewed. • Applications in natural product formation and synthetic approaches are provided.

show abstract

“…Siderophores, metal-complexing molecules of high affinity, are also produced by bacteria in biofilms (Visca et al, 2007;Saha et al, 2013). Siderophore production by bacteria, including the ligands catecholate, hydroxamate, and carboxylate, is extensively reviewed (Springer and Butler, 2016;Albelda-Berenguer et al, 2019), and present the central role of this class of molecules for metal scavenging. Other highly complexing ligands are also secreted by bacteria, such as cysteine-containing molecules and glutathione that exhibit thiol groups of high affinity toward soft metals (Brown et al, 2006;Mugerfeld et al, 2009).…”

Section: Ligand-mediated Dissolutionmentioning

confidence: 99%