A Structural and Functional Model for the 1‐Aminocyclopropane‐1‐carboxylic Acid Oxidase

Sallmann, Madleen; Oldenburg, Fabio; Braun, Beatrice; Réglier, Marius; Simaan, A. Jalila; Limberg, Christian

doi:10.1002/anie.201502529

Cited by 13 publications

(18 citation statements)

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“…Four miRNAs with targets involved in ethylene signal transduction were identified as being significantly different expression in all the continuously cultivated R. glutinosa roots. For example, miR2600a was further down-regulated in R3 and R4; its target is ACCS1, a gene encoding ACC oxidase, which is responsible for the final stage of ethylene synthesis (Sallmann et al, 2015;Somyong et al, 2016), an accumulation of ACCS1 would be expected to promote the ethylene synthesis. Furthermore, the down-regulation of miR5240b targeted the gene encoding ERTF, which underlie the positive regulation of ethylene-based signal transduction (Ohta et al, 2000;Shahin et al, 2016).…”

Section: Discussionmentioning

confidence: 99%

The miRNAomes in Rehmannia glutinosa Roots Exposed to Different Levels of Replanting Disease Pressure

Yang¹,

Li²,

Yan-jie³

2017

IJAB

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To cite this paper: Yang, Y., M. Li and Y. Yi, 2017. The miRNAomes in Rehmannia glutinosa roots exposed to different levels of replanting disease pressure. AbstractRoot development in the medicinal plant Rehmannia glutinosa is severely disordered by replanting disease, which occurs when it is grown in the same soils over consecutive seasons. Following the demonstration of changes to the miRNAome of the R. glutinosa plants in the second year of cultivation, a fuller experiment was organized to track the root miRNAomes over four successive plantings. Four small RNA libraries were generated from the roots of one year's planted (free of replanting disease) and 2-4 years' continuous cultivation (replanting disease) R. glutinosa plants, respectively. Sequencing of these libraries revealed the presence of 18 novel and 344 conserved miRNA families. The abundance of many of the miRNAs varied between the four libraries, consistent with the notion that replanting disease reflects the outcome differential miRNA transcription. A combined bioinformatic and degradome sequencing approach allowed the identification of 69 differentially abundant (DA) miRNA targets, leading to the recognition that particular miRNA/target modules may be important for the expression of the disease. The expression profiles of 28 key miRNAs and their targets implied that the longer years of continuous cultivation was extended, the more severe tendency of these profiles' changes would be. The indication was that the miRNAs-responsive continuous cultivation pressure reprogrammed gene expression patterns, which disordered hormone signaling, repressed core mechanisms, weakened stress tolerance and resulted in forming the disease in R. glutinosa. In conclusion, the key miRNAs involved in important roles of replanting disease and were a crucial basis for exploration in the disease forming repertoire.

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Section: Discussionmentioning

confidence: 99%

The miRNAomes in Rehmannia glutinosa Roots Exposed to Different Levels of Replanting Disease Pressure

Yang¹,

Li²,

Yan-jie³

2017

IJAB

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“…Inspired by the intriguing reaction catalyzed by ACCO, a number of iron and copper complexes employing polydentate nitrogen donor ligands have been reported to display H 2 O 2 ‐dependent ACCO‐like activity . In contrast, mononuclear iron(II)‐ACC complex is less explored , . So far, there is only one report on the iron(II)‐ACC complex that use dioxygen to emulate the activity of ACCO .…”

Section: Introductionmentioning

confidence: 99%

“…So far, there is only one report on the iron(II)‐ACC complex that use dioxygen to emulate the activity of ACCO . Limberg and co‐workers have synthesized an iron(II)‐ACC complex using a tris(pyrazolyl)borate ligand, which exhibited around 17 % ethylene formation with dioxygen at an elevated temperature . Unfortunately, the structure of the iron(II)‐ACC complex has not been reported.…”

Section: Introductionmentioning

confidence: 99%

“…[13][14][15][16][17][18] In contrast, mononuclear iron(II)-ACC complex is less explored. [18,19] So far, there is only one report on the iron(II)-ACC complex that use dioxygen to emulate the activity of ACCO. [20] Limberg and co-workers have synthesized an iron(II)-ACC complex using a tris(pyrazolyl)borate ligand, which exhibited around 17 % ethylene formation with dioxygen at an elevated temperature.…”

Section: Introductionmentioning

confidence: 99%

“…[20] Limberg and co-workers have synthesized an iron(II)-ACC complex using a tris(pyrazolyl)borate ligand, which exhibited around 17 % ethylene formation with dioxygen at an elevated temperature. [19] Unfortunately, the structure of the iron(II)-ACC complex has not been reported. The solid-state structure of a nickel analogue was used to put forward a possible structure of the iron(II) complex.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Bio‐inspired Oxidation of 1‐Aminocarboxylic Acids by a Nonheme Iron(II) Complex: Mimicking the Activity of 1‐Aminocyclopropane‐1‐carboxylic Acid Oxidase

Rahaman

Munshi

Paine

2018

Zeitschrift anorg allge chemie

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Three new ternary iron(II) complexes, [(TpPh2)FeII(ACC)] (1), [(TpPh2)FeII(ACH)] (2), and [(TpPh2)FeII(ADP)] (3) [TpPh2 = hydrotris(3,5‐diphenylpyrazol‐1‐yl)borate, ACC‐H = 1‐aminocyclopropane‐1‐carboxylic acid, ACH‐H = 1‐aminocyclohexane‐1‐carboxylic acid, and ADP‐H = 2‐amino‐2,2‐diphenylacetic acid] were isolated and characterized. X‐ray crystal structures of 1 and 2 reveal that in both the complexes the TpPh2 ligand binds to the central iron atom in a facial mode, and the respective 1‐aminocarboxylate monoanion displays bidentate binding mode through one carboxylate oxygen and one amine nitrogen donor. Complex 1 represents a structural model of the enzyme‐substrate adduct of the enzyme, 1‐aminocyclopropane‐1‐carboxylic acid oxidase (ACCO). The iron(II) complexes react with O2 at ambient temperature to convert the metal coordinated coligands to the corresponding carbonyl compound but in low yields. The yields of the decarboxylated products, however, increase upon increasing the reaction temperature. Isotope labelling experiments and interception studies indicate that the reductive activation of O2 at the central iron atom concomitant with two‐electron oxidative decarboxylation of the coligand following a pathway very similar to that proposed for the iron(II)‐α‐hydroxy acid complexes of the TpPh2 ligand.

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Enhancing Tris(pyrazolyl)borate‐Based Models of Cysteine/Cysteamine Dioxygenases through Steric Effects: Increased Reactivities, Full Product Characterization and Hints to Initial Superoxide Formation

Müller

Hoof

Keck

et al. 2020

Chemistry A European J

Self Cite

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The design of biomimetic model complexes for the cysteine dioxygenase (CDO) and cysteamine dioxygenase (ADO) is reported, where the 3‐His coordination of the iron ion is simulated by three pyrazole donors of a trispyrazolyl borate ligand (Tp) and protected cysteine and cysteamine represent substrate ligands. It is found that the replacement of phenyl groups—attached at the 3‐positions of the pyrazole units in a previous model—by mesityl residues has massive consequences, as the latter arrange to a more spacious reaction pocket. Thus, the reaction with O2 proceeds much faster and afterwards the first structural characterization of an iron(II) η2‐O,O‐sulfinate product became possible. If one of the three Tp‐mesityl groups is placed in the 5‐position, an even larger reaction pocket results, which leads to yet faster rates and accumulation of a reaction intermediate at low temperatures, as shown by UV/Vis and Mössbauer spectroscopy. After comparison with the results of investigations on the cobalt analogues this intermediate is tentatively assigned to an iron(III) superoxide species.

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A Structural and Functional Model for the 1‐Aminocyclopropane‐1‐carboxylic Acid Oxidase

Cited by 13 publications

References 48 publications

The miRNAomes in Rehmannia glutinosa Roots Exposed to Different Levels of Replanting Disease Pressure

The miRNAomes in Rehmannia glutinosa Roots Exposed to Different Levels of Replanting Disease Pressure

Bio‐inspired Oxidation of 1‐Aminocarboxylic Acids by a Nonheme Iron(II) Complex: Mimicking the Activity of 1‐Aminocyclopropane‐1‐carboxylic Acid Oxidase

Enhancing Tris(pyrazolyl)borate‐Based Models of Cysteine/Cysteamine Dioxygenases through Steric Effects: Increased Reactivities, Full Product Characterization and Hints to Initial Superoxide Formation

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