Flavodiiron Proteins and Their Role in Cyanobacteria

Gonçalves, Vera L.; Vicente, João B.; Saraiva, Lı́gia M.; Teixeira, Miguel

doi:10.1007/978-94-007-0388-9_22

Cited by 11 publications

(20 citation statements)

References 57 publications

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“…cyanobacteria and oxygenic photosynthetic eukaryotes were aligned with the sequences of prototypical FDPs, which were used as reference sequences. Two main clusters are obtained which is in agreement with previous analysis [16][17][18].…”

Section: Flv1 Has No-canonical Residues At the Di-iron Catalytic Sitesupporting

confidence: 91%

“…The dendrogram obtained (Figure 2A) clearly highlights that the FDPs are widely distributed, both in prokaryotes and eukaryotes, as observed previously [16].…”

Section: Flv1 Has No-canonical Residues At the Di-iron Catalytic Sitesupporting

confidence: 82%

“…The sequences of The numbers 1-12 correspond to the type of ligands of the di-iron catalytic site of the proteins. For more details, see [16].…”

Section: Flv1 Has No-canonical Residues At the Di-iron Catalytic Sitementioning

confidence: 99%

“…Our analysis, presented in Figure 2(B), revealed that 50 % of the aligned sequences have conserved residues precisely matching the canonical ones known to be involved in iron coordination (H 81 -X-E 83 -X-D 85 -H 86 -X 61 -H 148 -X 18 -D 167 -X 60 -H 228 , Moorella thermoacetica numbering). These sequences that were designated as class C type 1 FDPs include the Flv3 and Flv4 proteins from Synechocystis [16]. The remaining 50 % of the sequences showed, surprisingly, a high number of possible ligand combinations, types 2-12.…”

Section: Flv1 Has No-canonical Residues At the Di-iron Catalytic Sitementioning

confidence: 99%

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Gene expression study of the flavodi-iron proteins from the cyanobacterium Synechocystis sp. PCC6803

Gonçalves

Saraiva

Teixeira

2011

Biochemical Society Transactions

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The flavodi-iron proteins, also named FDPs, are an extensive family of enzymes able to reduce dioxygen to water and/or nitric oxide to nitrous oxide. These proteins are formed by a metallo-β-lactamase-like module with a di-iron catalytic site fused to a flavodoxin-like module bearing an FMN. However, in cyanobacteria, which are oxygenic photosynthetic organisms widespread in Nature, FDPs have an extra NAD(P)H:flavin reductase-like domain as a C-terminal extension. Interestingly, cyanobacteria contain more than one gene encoding FDP-like proteins, with the genome of Synechocystis sp. PCC6803 containing four genes coding for putative FDPs. However, the function of those proteins remains unclear. In the present study, we have analysed the expression profile of these genes under oxidative and nitrosative stress conditions. The results indicate that one of the flavodi-iron genes, the so-called flv1, is induced in cells exposed to nitrosative stress. By conducting a broad analysis on the primary sequences of FDPs, we have identified that the FDPs of cyanobacteria and oxygenic photosynthetic eukaryotes may be divided into multiple types (1-12), according to the amino acid residues of the di-iron catalytic site.

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Section: Flv1 Has No-canonical Residues At the Di-iron Catalytic Sitesupporting

confidence: 91%

“…The dendrogram obtained (Figure 2A) clearly highlights that the FDPs are widely distributed, both in prokaryotes and eukaryotes, as observed previously [16].…”

Section: Flv1 Has No-canonical Residues At the Di-iron Catalytic Sitesupporting

confidence: 82%

“…The sequences of The numbers 1-12 correspond to the type of ligands of the di-iron catalytic site of the proteins. For more details, see [16].…”

Section: Flv1 Has No-canonical Residues At the Di-iron Catalytic Sitementioning

confidence: 99%

Section: Flv1 Has No-canonical Residues At the Di-iron Catalytic Sitementioning

confidence: 99%

See 2 more Smart Citations

Gene expression study of the flavodi-iron proteins from the cyanobacterium Synechocystis sp. PCC6803

Gonçalves

Saraiva

Teixeira

2011

Biochemical Society Transactions

Self Cite

View full text Add to dashboard Cite

show abstract

“…We detected several cofactors of interest (Figure S14); however, the length and treatment conditions utilized in the metabolite may not be suitable for unstable metabolites, such as NADH and NADPH, and thus no conclusions are made about the temporal profile of these metabolites as detected here. Flavin mononucleotide (FMN) accumulation peaks during mid‐day, consistent with a hypothesis of increased demand during periods of high oxidative stress (Gonçalves et al ., ). Guanosine triphosphate (GTP), a precursor for the synthesis of FMN and other cofactors, peaks early in the day to support increased demand for FMN.…”

Section: Resultsmentioning

confidence: 97%

A comprehensive time‐course metabolite profiling of the model cyanobacterium Synechocystis sp. PCC 6803 under diurnal light:dark cycles

et al. 2019

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Cyanobacteria are a model photoautotroph and a chassis for the sustainable production of fuels and chemicals. Knowledge of photoautotrophic metabolism in the natural environment of day/night cycles is lacking, yet has implications for improved yield from plants, algae and cyanobacteria. Here, a thorough approach to characterizing diverse metabolites-including carbohydrates, lipids, amino acids, pigments, cofactors, nucleic acids and polysaccharides-in the model cyanobacterium Synechocystis sp. PCC 6803 (S. 6803) under sinusoidal diurnal light:dark cycles was developed and applied. A custom photobioreactor and multiplatform mass spectrometry workflow enabled metabolite profiling every 30-120 min across a 24-h diurnal sinusoidal LD ('sinLD') cycle peaking at 1600 lmol photons m À2 sec À1 . We report widespread oscillations across the sinLD cycle with 90%, 94% and 40% of the identified polar/semi-polar, non-polar and polymeric metabolites displaying statistically significant oscillations, respectively. Microbial growth displayed distinct lag, biomass accumulation and cell division phases of growth. During the lag phase, amino acids and nucleic acids accumulated to high levels per cell followed by decreased levels during the biomass accumulation phase, presumably due to protein and DNA synthesis. Insoluble carbohydrates displayed sharp oscillations per cell at the day-to-night transition. Potential bottlenecks in central carbon metabolism are highlighted. Together, this report provides a comprehensive view of photosynthetic metabolite behavior with high temporal resolution, offering insight into the impact of growth synchronization to light cycles via circadian rhythms. Incorporation into computational modeling and metabolic engineering efforts promises to improve industrially relevant strain design.

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The dual function of flavodiiron proteins: oxygen and/or nitric oxide reductases

et al. 2016

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Flavodiiron proteins have emerged in the last two decades as a newly discovered family of oxygen and/or nitric oxide reductases widespread in the three life domains, and present in both aerobic and anaerobic organisms. Herein we present the main features of these fascinating enzymes, with a particular emphasis on the metal sites, as more appropriate for this special issue in memory of the exceptional bioinorganic scientist R. J. P. Williams who pioneered the notion of (metal) element availability-driven evolution. We also compare the flavodiiron proteins with the other oxygen and nitric oxide reductases known until now, highlighting how throughout evolution Nature arrived at different solutions for similar functions, in some cases adding extra features, such as energy conservation. These enzymes are an example of the (bioinorganic) unpredictable diversity of the living world.

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Flavodiiron Proteins and Their Role in Cyanobacteria

Cited by 11 publications

References 57 publications

Gene expression study of the flavodi-iron proteins from the cyanobacterium Synechocystis sp. PCC6803

Gene expression study of the flavodi-iron proteins from the cyanobacterium Synechocystis sp. PCC6803

A comprehensive time‐course metabolite profiling of the model cyanobacterium Synechocystis sp. PCC 6803 under diurnal light:dark cycles

The dual function of flavodiiron proteins: oxygen and/or nitric oxide reductases

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