Snapshots of PLP‐substrate and PLP‐product external aldimines as intermediates in two types of cysteine desulfurase enzymes

Nakamura, Ryosuke; Hikita, Masahide; Ogawa, Sachiko; Takahashi, Yasuhiro; Fujishiro, Takashi

doi:10.1111/febs.15081

Cited by 20 publications

(34 citation statements)

References 50 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…PLP-dependent enzymes form a huge family that perform various types of elimination and substitution reactions on amino acids and their derivatives. Several structures of cysteine desulfurase have been solved and all revealed an arrangement as homodimers, in which the PLP-binding pocket of one subunit is completed by the second one (Figure 3A,B) [39,67,[144][145][146][147][148][149][150]. Cysteine desulfurases also display key differences allowing their categorization in two classes owing to the length of the mobile loop carrying their catalytic cysteine [39].…”

Section: Two Different Classes Of Cysteine Desulfurasementioning

confidence: 99%

Mechanism of Iron–Sulfur Cluster Assembly: In the Intimacy of Iron and Sulfur Encounter

et al. 2020

View full text Add to dashboard Cite

Iron–sulfur (Fe–S) clusters are protein cofactors of a multitude of enzymes performing essential biological functions. Specialized multi-protein machineries present in all types of organisms support their biosynthesis. These machineries encompass a scaffold protein on which Fe–S clusters are assembled and a cysteine desulfurase that provides sulfur in the form of a persulfide. The sulfide ions are produced by reductive cleavage of the persulfide, which involves specific reductase systems. Several other components are required for Fe–S biosynthesis, including frataxin, a key protein of controversial function and accessory components for insertion of Fe–S clusters in client proteins. Fe–S cluster biosynthesis is thought to rely on concerted and carefully orchestrated processes. However, the elucidation of the mechanisms of their assembly has remained a challenging task due to the biochemical versatility of iron and sulfur and the relative instability of Fe–S clusters. Nonetheless, significant progresses have been achieved in the past years, using biochemical, spectroscopic and structural approaches with reconstituted system in vitro. In this paper, we review the most recent advances on the mechanism of assembly for the founding member of the Fe–S cluster family, the [2Fe2S] cluster that is the building block of all other Fe–S clusters. The aim is to provide a survey of the mechanisms of iron and sulfur insertion in the scaffold proteins by examining how these processes are coordinated, how sulfide is produced and how the dinuclear [2Fe2S] cluster is formed, keeping in mind the question of the physiological relevance of the reconstituted systems. We also cover the latest outcomes on the functional role of the controversial frataxin protein in Fe–S cluster biosynthesis.

show abstract

Section: Two Different Classes Of Cysteine Desulfurasementioning

confidence: 99%

Mechanism of Iron–Sulfur Cluster Assembly: In the Intimacy of Iron and Sulfur Encounter

et al. 2020

View full text Add to dashboard Cite

show abstract

“…D-cysteine desulfurases in the soil planted with C. cajan were decreased (4657 in the surface soil and 2675 in the mixed soil of coal and gangue). Nitrogen monoxide is an inevitable intermediate product in the denitrification process and is also a cytotoxin [ 36 37 ]. If a large amount of accumulation threatens the life of cells, nitric-oxide reductase can reduce nitric oxide to nontoxic nitrous oxide, which plays an essential role in biological nitrogen removal [43].…”

Section: Resultsmentioning

confidence: 99%

Investigation of bacterial diversity in Cajanus cajan -planted gangue soil via high-throughput sequencing

Han

Wang

et al. 2021

Bioengineered

View full text Add to dashboard Cite

The ecological restoration of coal gangue can be achieved by planting Cajanus cajan (pigeon pea) because of its developed root system. The close relationships soil microorganisms have with plants are crucial for improving soil composition; the soil composition affects nutrient absorption. The microbial composition and function of soil planted with C. cajan in reclaimed land were compared with soil that was not planted with C. cajan (the control). Results showed that the dominant microflora in the soil significantly changed after planting C. cajan. Before planting, the dominant microflora included members of the phyla Sulfobacteria and Acidobacteria. After planting, the dominant microflora contained bacteria from phyla and classes that included Actinobacteria, Acidimicubia, Thermoleophilia, and Anaerolineae. Additionally, there were significant differences in the bacterial composition of each layer in soils planted with C. cajan. Principal component analysis revealed that the interpretation degrees of the results for PC2 and PC3 axes were 10.46% and 3.87%, respectively. The dominant microflora were Vicinamibacterales, Nocardioides, and Arthrobacter in the surface soil; Actinophytocola and Sphingomonas in the deep soil; and Sulfobacillus and Acidimicrobium in the mixed-layer soil. Function prediction analysis using the bioinformatics software package PICRUSt revealed that the abundance of operational taxonomic units corresponding to sigma 54-specific transcriptional regulators, serine threonine protein kinase, and histidine kinase increased by 111.2%, 56.8%, and 47.4%, respectively, after planting C. cajan. This study provides a reference for interactions among microorganisms in reclaimed soils for guiding the development and restoration of waste coal gangue hills.

show abstract

“…A particularly recognized structural difference between type I and type II is the catalytic loop, which contains a nucleophilic cysteine. This catalytic loop of type I cysteine desulfurases is longer than that of type II enzymes and, therefore, it is considered to be structurally more flexible than that of type II enzymes [55][56][57].…”

Section: Cysteine Desulfurasesmentioning

confidence: 99%

Fe-S Protein Synthesis in Green Algae Mitochondria

Gómez-Casati

Busi

Barchiesi

et al. 2021

Plants

View full text Add to dashboard Cite

Iron and sulfur are two essential elements for all organisms. These elements form the Fe-S clusters that are present as cofactors in numerous proteins and protein complexes related to key processes in cells, such as respiration and photosynthesis, and participate in numerous enzymatic reactions. In photosynthetic organisms, the ISC and SUF Fe-S cluster synthesis pathways are located in organelles, mitochondria, and chloroplasts, respectively. There is also a third biosynthetic machinery in the cytosol (CIA) that is dependent on the mitochondria for its function. The genes and proteins that participate in these assembly pathways have been described mainly in bacteria, yeasts, humans, and recently in higher plants. However, little is known about the proteins that participate in these processes in algae. This review work is mainly focused on releasing the information on the existence of genes and proteins of green algae (chlorophytes) that could participate in the assembly process of Fe-S groups, especially in the mitochondrial ISC and CIA pathways.

show abstract

Snapshots of PLP‐substrate and PLP‐product external aldimines as intermediates in two types of cysteine desulfurase enzymes

Cited by 20 publications

References 50 publications

Mechanism of Iron–Sulfur Cluster Assembly: In the Intimacy of Iron and Sulfur Encounter

Mechanism of Iron–Sulfur Cluster Assembly: In the Intimacy of Iron and Sulfur Encounter

Investigation of bacterial diversity in Cajanus cajan -planted gangue soil via high-throughput sequencing

Fe-S Protein Synthesis in Green Algae Mitochondria

Contact Info

Product

Resources

About