Final Electron Acceptor Research Articles

Two marine sulfur-reducing bacteria co-culture is essential for productive infection by a T4-like Escherichia coli-infecting phage

The control of microbiologically influenced corrosion (MIC) challenges the oil exploration sector. The MIC results from electrochemical reactions facilitated by microorganisms such as sulfate-reducing bacteria (SRB), which adhere to the surface of the ducts forming biofilms. SRB uses sulfate as the final electron acceptor, resulting in hydrogen sulfide as the final product, a highly reactive corrosive, and toxic compound. Due to the high diversity of the SRB group, this study evaluated the effect of an Escherichia coli phage, with biofilm degrading enzymes, in preventing biofilm formation by microbial consortium P48SEP and reducing H2S production in a complex SRB community. Three phage concentrations were evaluated (104, 108 and 1012 UFP/ml). High and medium phage concentrations prevented biofilm development, as evidenced by scanning electron microscopy, chemical analysis, and cell counts. In addition, the virus altered the expression pattern of some bacterial genes and the relative abundance of proteins related to biofilm formation and cell stress response. Using a complex culture formed mainly by SRB, it was possible to observe the bacterial growth, H2S, and metabolic activity reduction after the phage was added. This study shows for the first time the ability of an E. coli-infecting phage to prevent the biofilm formation of an SRB consortium and infect and replicate at high concentrations on the non-specific host. This new finding turns the use of non-specific phages a promising alternative for the control of biocorrosion in oil and gas installations, on the other side, alert to the use of large concentration of phages and the influence on bacterial groups with geological importance, opening a research field in phage biology.

Rhodoquinone-dependent electron transport chain is essential for Caenorhabditis elegans survival in hydrogen sulfide environments

Hydrogen sulfide (H2S) has traditionally been considered as an environmental toxin for animal lineages; yet, it plays a signaling role in various processes at low concentrations. Mechanisms controlling H2S in animals, especially in sulfide-rich environments, are not fully understood. The main detoxification pathway involves the conversion of H2S into less harmful forms, through a mitochondrial oxidation pathway. The first step of this pathway oxidizes sulfide and reduces ubiquinone (UQ) through sulfide-quinone oxidoreductase (SQRD/SQOR). Because H2S inhibits cytochrome oxidase and hence UQ regeneration, this pathway becomes compromised at high H2S concentrations. The free-living nematode C. elegans feeds on bacteria and can face high sulfide concentrations in its natural environment. This organism has an alternative ETC that uses rhodoquinone (RQ) as the lipidic electron transporter and fumarate as the final electron acceptor. In this study, we demonstrate that RQ is essential for survival in sulfide. RQ-less animals (kynu-1 and coq-2e KO) cannot survive high H2S concentrations, while UQ-less animals (clk-1 and coq-2a KO) exhibit recovery, even when provided with a UQ-deficient diet. Our findings highlight that sqrd-1 uses both benzoquinones and that RQ-dependent ETC confers a key advantage (RQ regeneration) over UQ in sulfide-rich conditions. C. elegans also faces cyanide, another cytochrome oxidase inhibitor, whose detoxification leads to H2S production, via cysl-2. Our study reveals that RQ delays killing by the HCN-producing bacteria Pseudomonas aeruginosa PAO1. These results underscore the fundamental role that RQ-dependent ETC serves as a biochemical adaptation to H2S environments, and to pathogenic bacteria producing cyanide and H2S toxins.

X-ray structure and enzymatic study of a bacterial NADPH oxidase highlight the activation mechanism of eukaryotic NOX.

NADPH oxidases (NOX) are transmembrane proteins, widely spread in eukaryotes and prokaryotes, that produce reactive oxygen species (ROS). Eukaryotes use the ROS products for innate immune defense and signaling in critical (patho)physiological processes. Despite the recent structures of human NOX isoforms, the activation of electron transfer remains incompletely understood. SpNOX, a homolog from Streptococcus pneumoniae, can serves as a robust model for exploring electron transfers in the NOX family thanks to its constitutive activity. Crystal structures of SpNOX full-length and dehydrogenase (DH) domain constructs are revealed here. The isolated DH domain acts as a flavin reductase, and both constructs use either NADPH or NADH as substrate. Our findings suggest that hydride transfer from NAD(P)H to FAD is the rate-limiting step in electron transfer. We identify significance of F397 in nicotinamide access to flavin isoalloxazine and confirm flavin binding contributions from both DH and Transmembrane (TM) domains. Comparison with related enzymes suggests that distal access to heme may influence the final electron acceptor, while the relative position of DH and TM does not necessarily correlate with activity, contrary to previous suggestions. It rather suggests requirement of an internal rearrangement, within the DH domain, to switch from a resting to an active state. Thus, SpNOX appears to be a good model of active NOX2, which allows us to propose an explanation for NOX2's requirement for activation.

X-ray structure and enzymatic study of a bacterial NADPH oxidase highlight the activation mechanism of eukaryotic NOX

NADPH oxidases (NOX) are transmembrane proteins, widely spread in eukaryotes and prokaryotes, that produce reactive oxygen species (ROS). Eukaryotes use the ROS products for innate immune defense and signaling in critical (patho)physiological processes. Despite the recent structures of human NOX isoforms, the activation of electron transfer remains incompletely understood. SpNOX, a homolog from Streptococcus pneumoniae, can serves as a robust model for exploring electron transfers in the NOX family thanks to its constitutive activity. Crystal structures of SpNOX full-length and dehydrogenase (DH) domain constructs are revealed here. The isolated DH domain acts as a flavin reductase, and both constructs use either NADPH or NADH as substrate. Our findings suggest that hydride transfer from NAD(P)H to FAD is the rate-limiting step in electron transfer. We identify significance of F397 in nicotinamide access to flavin isoalloxazine and confirm flavin binding contributions from both DH and Transmembrane (TM) domains. Comparison with related enzymes suggests that distal access to heme may influence the final electron acceptor, while the relative position of DH and TM does not necessarily correlate with activity, contrary to previous suggestions. It rather suggests requirement of an internal rearrangement, within the DH domain, to switch from a resting to an active state. Thus, SpNOX appears to be a good model of active NOX2, which allows us to propose an explanation for NOX2’s requirement for activation.

Spatial adjustment of bioenergetics, a possible determinant of contractile adaptation and development of contractile failure.

Cardiomyocytes depend on mitochondrial oxidative phosphorylation (OXPHOS) for energy metabolism, which is facilitated by the mitochondrial electron transfer system (ETS). In a series of thermogenic redox reactions, electrons are shuttled through the ETS to oxygen as the final electron acceptor. This electron transfer is coupled to proton translocation across the inner mitochondrial membrane, which itself is the main driving force for ATP production. Oxygen availability is thus a prerequisite for ATP production and consequently contractility. Notably, cardiomyocytes are exceptionally large cells and densely packed with contractile structures, which constrains intracellular oxygen distribution. Moreover, oxygen must pass through layers of actively respiring mitochondria to reach the ones located in the innermost contractile compartment. Indeed, uneven oxygen distribution was observed in cardiomyocytes, suggesting that local ATP supply may also vary according to oxygen availability. Here, we discuss how spatial adjustment of bioenergetics to intracellular oxygen fluctuations may underlie cardiac contractile adaptation and how this adaptation may pose a risk for the development of contractile failure.

Long-term continuous degradation of carbon nanotubes by a bacteria-driven Fenton reaction

Very few bacteria are known that can degrade carbon nanotubes (CNTs), and the only known degradation mechanism is a Fenton reaction driven by Labrys sp. WJW with siderophores, which only occurs under iron-deficient conditions. No useful information is available on the degradation rates or long-term stability and continuity of the degradation reaction although several months or more are needed for CNT degradation. In this study, we investigated long-term continuous degradation of oxidized (carboxylated) single-walled CNTs (O-SWCNTs) using bacteria of the genus Shewanella. These bacteria are widely present in the environment and can drive the Fenton reaction by alternating anaerobic-aerobic growth conditions under more general environmental conditions. We first examined the effect of O-SWCNTs on the growth of S. oneidensis MR-1, and it was revealed that O-SWCNTs promote growth up to 30 μg/mL but inhibit growth at 40 μg/mL and above. Then, S. oneidensis MR-1 was subjected to incubation cycles consisting of 21-h anaerobic and 3-h aerobic periods in the presence of 30 μg/mL O-SWCNTs and 10 mM Fe(III) citrate. We determined key factors that help prolong the bacteria-driven Fenton reaction and finally achieved long-term continuous degradation of O-SWCNTs over 90 d. By maintaining a near neutral pH and replenishing Fe(III) citrate at 60 d, a degraded fraction of 56.3% was reached. S. oneidensis MR-1 produces Fe(II) from Fe(III) citrate, a final electron acceptor for anaerobic respiration during the anaerobic period. Then, ·OH is generated through the Fenton reaction by Fe(II) and H2O2 produced by MR-1 during the aerobic period. ·OH was responsible for O-SWCNT degradation, which was inhibited by scavengers of H2O2 and ·OH. Raman spectroscopy and X-ray photoelectron spectroscopy showed that the graphitic structure in O-SWCNTs was oxidized, and electron microscopy showed that long CNT fibers initially aggregated and became short and isolated during degradation. Since Shewanella spp. and iron are ubiquitous in the environment, this study suggests that a Fenton reaction driven by this genus is applicable to the degradation of CNTs under a wide range of conditions and will help researchers develop novel methods for waste treatment and environmental bioremediation against CNTs.

Supersulfide biology and translational medicine for disease control.

For decades, the major focus of redox biology has been oxygen, the most abundant element on Earth. Molecular oxygen functions as the final electron acceptor in the mitochondrial respiratory chain, contributing to energy production in aerobic organisms. In addition, oxygen-derived reactive oxygen species including hydrogen peroxide and nitrogen free radicals, such as superoxide, hydroxyl radical and nitric oxide radical, undergo a complicated sequence of electron transfer reactions with other biomolecules, which lead to their modified physiological functions and diverse biological and pathophysiological consequences (e.g. oxidative stress). What is now evident is that oxygen accounts for only a small number of redox reactions in organisms and knowledge of biological redox reactions is still quite limited. This article reviews a new aspects of redox biology which is governed by redox-active sulfur-containing molecules-supersulfides. We define the term 'supersulfides' as sulfur species with catenated sulfur atoms. Supersulfides were determined to be abundant in all organisms, but their redox biological properties have remained largely unexplored. In fact, the unique chemical properties of supersulfides permit them to be readily ionized or radicalized, thereby allowing supersulfides to actively participate in redox reactions and antioxidant responses in cells. Accumulating evidence has demonstrated that supersulfides are indispensable for fundamental biological processes such as energy production, nucleic acid metabolism, protein translation and others. Moreover, manipulation of supersulfide levels was beneficial for pathogenesis of various diseases. Thus, supersulfide biology has opened a new era of disease control that includes potential applications to clinical diagnosis, prevention and therapeutics of diseases.

Structure and function of the S. pombe III-IV-cyt c supercomplex.

The respiratory chain in aerobic organisms is composed of a number of membrane-bound protein complexes that link electron transfer to proton translocation across the membrane. In mitochondria, the final electron acceptor, complex IV (CIV), receives electrons from dimeric complex III (CIII2), via a mobile electron carrier, cytochrome c. In the present study, we isolated the CIII2CIV supercomplex from the fission yeast Schizosaccharomyces pombe and determined its structure with bound cyt. c using single-particle electron cryomicroscopy. A respiratory supercomplex factor 2 was found to be bound at CIV distally positioned in the supercomplex. In addition to the redox-active metal sites, we found a metal ion, presumably Zn2+, coordinated in the CIII subunit Cor1, which is encoded by the same gene (qcr1) as the mitochondrial-processing peptidase subunit β. Our data show that the isolated CIII2CIV supercomplex displays proteolytic activity suggesting a dual role of CIII2 in S. pombe. As in the supercomplex from S. cerevisiae, subunit Cox5 of CIV faces towards one CIII monomer, but in S. pombe, the two complexes are rotated relative to each other by ~45°. This orientation yields equal distances between the cyt. c binding sites at CIV and at each of the two CIII monomers. The structure shows cyt. c bound at four positions, but only along one of the two symmetrical branches. Overall, this combined structural and functional study reveals the integration of peptidase activity with the CIII2 respiratory system and indicates a two-dimensional cyt. c diffusion mechanism within the CIII2-CIV supercomplex.

Cellulose-fueled microbial fuel cells equipped with a bipolar membrane using hydrogen phosphate as the final electron acceptor.

A bipolar membrane microbial fuel cell (bMFC) is used to generate electricity using cellulose in phosphate buffer solution as fuel, and the mechanism of electricity generation is elucidated from five reference experiments. The bMFC was operated for 20 days using cellulose as fuel and Cellulomonas fimi. In the first reference experiment, no microorganism was used. In the second experiment, a cation-exchange membrane was used instead of a bipolar membrane. In the third experiment, the bipolar membrane was used in the opposite orientation as in the main experiment. In the fourth experiment, D2O was used instead of H2O in the cathode chamber. In the final experiment, the tris-maleate buffer was used instead of a phosphate buffer. Sufficient power generation did not occur in either reference experiment. The bMFC continuously generated electricity for 20days, and elucidated H+ and OH- react in bipolar membrane, where the counter cation of dihydrogen phosphate served as the final electron acceptor.

Compost-derived humic and fulvic acid coupling with Shewanella oneidensis MR-1 for the bioreduction of Cr(Ⅵ)

The compost-derived humic acids (HA) and fulvic acids (FA) contain abundant active functional groups with strong redox capacity, which can function as an electron shuttles for promoting the reduction of heavy metals, thus changing the form of the pollutants in the environment and reducing their toxicity. Therefore, in this study, UV–Vis, FTIR, 3D-EEM, electrochemical analysis were applied to study the spectral characteristics and electron transfer capacity (ETC) of HA and FA. Upon analysis, the results showed an increasing trend of ETC and humification degree (SUVA254) for both HA and FA during composting. However, the aromatic degree (SUVA280) of HA was higher than FA. After 7 days of culture, 37.95% of Cr (Ⅵ) was reduced by Shewanella oneidensis MR-1 (MR-1) alone. Whereas, only if HA or FA existed, the diminution of Cr (Ⅵ) reached 37.43% and 40.55%, respectively. However, the removal rate of Cr (Ⅵ) by HA/MR-1 and FA/MR-1 increased to 95.82% and 93.84% respectively. It indicated that HA and FA acted as electron shuttles, mediating the transfer of electrons between MR-1 and the final electron acceptor, effectively facilitating the bioreduction of Cr (Ⅵ) to Cr (Ⅲ) and also determined via correlation analysis. This study suggested compost-derived HA and FA coupling with MR-1 exhibited excellent performance for the bioreduction of Cr (Ⅵ) to Cr (Ⅲ).

Starvation combined with constant anode potential triggers intracellular electron storage in electro-active biofilms

The accumulation of electrons in the form of Extracellular Polymeric Substances (EPS) and poly-hydroxyalkanoates (PHA) has been studied in anaerobic processes by adjusting the access of microorganisms to the electron donor and final electron acceptor. In Bio-electrochemical systems (BESs), intermittent anode potential regimes have also recently been used to study electron storage in anodic electro-active biofilms (EABfs), but the effect of electron donor feeding mode on electron storage has not been explored. Therefore, in this study, the accumulation of electrons in the form of EPS and PHA was studied as a function of the operating conditions. EABfs were grown under both constant and intermittent anode potential regimes and fed with acetate (electron donor) continuously or in batch. Confocal Laser Scanning Microscopy (CLSM) and Fourier-Transform Infrared Spectroscopy (FTIR) were used to assess electron storage. The range of Coulombic efficiencies, from 25 to 82%, and the biomass yields, between 10 and 20%, indicate that storage could have been an alternative electron consuming process. From image processing, a 0.92 pixel ratio of poly-hydroxybutyrate (PHB) and amount of cells was found in the batch fed EABf grown under a constant anode potential. This storage was linked to the presence of living Geobacter and shows that energy gain and carbon source starvation were the triggers for intracellular electron storage. The highest EPS content (extracellular storage) was observed in the continuously fed EABf under an intermittent anode potential, showing that constant access to electron donor and intermittent access to the electron acceptor leads to the formation of EPS from the excess energy gained. Tailoring operating conditions can thus steer the microbial community and result in a trained EABf to perform a desired biological conversion, which can be beneficial for a more efficient and optimized BES.

Metabolic changes associated with dark-induced leaf senescence in Arabidopsis nadk2 mutants

ABSTRACT Arabidopsis NADK2 (NAD kinase 2) is a chloroplast-localized enzyme involved in NADP+ synthesis, which acts as the final electron acceptor in the photosynthetic electron transfer chain. The NADK2-deficient mutant (nadk2) was used to analyze the effect of NAD(P)(H) unbalance in the dark-induced leaf senescence. During senescence, WT plants and nadk2 mutants showed a similar reduction in chlorophyll content. NAD(P)(H) quantification showed that the amount of total NAD(P)(H) decreased on the day 7 in WT but on the day 3 in nadk2. The phosphorylation ratio (i.e. NADP(H)/NAD(H)) decreased on day 1 in WT. In contrast, the nadk2 showed lower phosphorylation ratio at 0 day and no change throughout the aging process. Metabolome analysis showed that the metabolic profiles of both WT plants and nadk2 mutants subjected to dark-induced senescence adopted similar patterns as the senescence progressed. However, the changes in individual metabolites in the nadk2 mutants were different from those of the WT during dark-induced senescence.

Redox control of tumor cell apoptosis during hypoxia

Currently, close attention is paid to studies aimed at searching for redox-sensitive targets for the regulation of tumor cell death. Tumor growth is characterized by impaired cell proliferation, differentiation, and apoptosis against the background of oxidative stress. Hypoxia contributes to the formation of mitochondrial dysfunction and acts as an additional factor that exacerbates oxidative stress in the tumor cell. Reactive oxygen species are general damaging factors, however, they can act as modulators of processes such as reception, intracellular signaling, proliferation, apoptosis, while taking part in the functioning of the cell redox system and contributing to the oxidative modification of macromolecules. One of the possible reasons for the activation of the production of reactive oxygen species is the low content of O2 in the cell, the final electron acceptor to ensure the functioning of the enzymes of the mitochondrial respiratory chain. The glutathione system makes a significant contribution to maintaining the balance between prooxidants and antioxidants in the cell. The role of this system is justified by the reduction potential of glutathione, which, acting as an acceptor of hydroxyl ions and singlet oxygen, significantly reduces the cytotoxic and damaging effects of reactive oxygen species. At the same time, it serves as a coenzyme for glutathione-dependent enzymes, which play a leading role not only in providing antioxidant processes, but also in maintaining the thiol disulfide balance. Hypoxia, which acts as a factor in the activation of free radical oxidation against the background of proliferation and apoptosis dysregulation, contributes to the formation of resistance of tumor cells to chemotherapeutic effects. In light of this, the importance of studying the redox-dependent mechanisms involved in the regulation and implementation of tumor cell death under insufficient oxygen supply becomes obvious, which is necessary for the development of personalized antitumor therapy. The article presents a review of modern literature, including the results of our own research, on the role of the thiol disulfide system and oxidatively modified proteins in the redox regulation of proliferation and apoptotic death of tumor cells, including under hypoxic conditions.

Oxidative phosphorylation in bone cells

The role of energy metabolism in bone cells is an active field of investigation. Bone cells are metabolically very active and require high levels of energy in the form of adenosine triphosphate (ATP) to support their function. ATP is generated in the cytosol via glycolysis coupled with lactic acid fermentation and in the mitochondria via oxidative phosphorylation (OXPHOS). OXPHOS is the final convergent metabolic pathway for all oxidative steps of dietary nutrients catabolism. The formation of ATP is driven by an electrochemical gradient that forms across the mitochondrial inner membrane through to the activity of the electron transport chain (ETC) complexes and requires the presence of oxygen as the final electron acceptor. The current literature supports a model in which glycolysis is the main source of energy in undifferentiated mesenchymal progenitors and terminally differentiated osteoblasts, whereas OXPHOS appears relevant in an intermediate stage of differentiation of those cells. Conversely, osteoclasts progressively increase OXPHOS during differentiation until they become multinucleated and mitochondrial-rich terminal differentiated cells. Despite the abundance of mitochondria, mature osteoclasts are considered ATP-depleted, and the availability of ATP is a critical factor that regulates the low survival capacity of these cells, which rapidly undergo death by apoptosis. In addition to ATP, bioenergetic metabolism generates reactive oxygen species (ROS) and intermediate metabolites that regulate a variety of cellular functions, including epigenetics changes of genomic DNA and histones. This review will briefly discuss the role of OXPHOS and the cross-talks OXPHOS-glycolysis in the differentiation process of bone cells.

Role of C/N ratio in a pilot scale Microbial Electrolysis Cell (MEC) for biomethane production and biogas upgrading

Microbial electrolysis cells (MECs) permit to couple the oxidation of waste organic streams (e.g., wastewater, fermentate or digestate) with the reduction of carbon dioxide into products with a high market value (e.g., methane or acetic acid). MECs exploit the ability of electroactive microorganisms to use a solid electrode as final electron acceptor or donor. Here, a micro pilot tubular MEC has been set up combining the anodic oxidation of the organic matter with the bioelectromethanogenesis reaction in the cathodic chamber. Seven different synthetic feeding solutions, simulating a domestic wastewater or an acidogenic fermentate, have been used to test different C/N ratio on the performance of the MEC bioanode in the range between 25 and 0.4 (molC/molN). As a main result it was found that, under the same operating conditions (i.e., anode potential controlled at + 0.2 V vs SHE and HRT of 0.5 d), a high C/N ratio (e.g., 19 mol/mol) promotes the bioelectrochemical metabolism of the electroactive biofilm. These findings are relevant for a practical application of the technology considering the variable content of carbon and nitrogen in real feedstocks.

Analysis of the external signals driving the transcriptional regulation of the main genes involved in denitrification in Haloferax mediterranei.

Haloferax mediterranei is the model microorganism for the study of the nitrogen cycle in haloarchaea. This archaeon not only assimilate N-species such as nitrate, nitrite, or ammonia, but also it can perform denitrification under low oxygen conditions, using nitrate or nitrite as alternative electron acceptors. However, the information currently available on the regulation of this alternative respiration in this kind of microorganism is scarce. Therefore, in this research, the study of haloarchaeal denitrification using H. mediterranei has been addressed by analyzing the promoter regions of the four main genes of denitrification (narGH, nirK, nor, and nosZ) through bioinformatics, reporter gene assays under oxic and anoxic conditions and by site-directed mutagenesis of the promoter regions. The results have shown that these four promoter regions share a common semi-palindromic motif that plays a role in the control of the expression levels of nor and nosZ (and probably nirK) genes. Regarding the regulation of the genes under study, it has been concluded that nirK, nor, and nosZ genes share some expression patterns, and therefore their transcription could be under the control of the same regulator whereas nar operon expression displays differences, such as the activation by dimethyl sulfoxide with respect to the expression in the absence of an electron acceptor, which is almost null under anoxic conditions. Finally, the study with different electron acceptors demonstrated that this haloarchaea does not need complete anoxia to perform denitrification. Oxygen concentrations around 100 μM trigger the activation of the four promoters. However, a low oxygen concentration per se is not a strong signal to activate the promoters of the main genes involved in this pathway; high activation also requires the presence of nitrate or nitrite as final electron acceptors.

Microbial Fuel Cell Equipped with Bipolar Membrane Using Iron (III) Hydroxide as Final Electron Acceptor

In this paper, we presented a novel microbial fuel cell (bMFC) structure, with a bipolar membrane separating the anode and cathode chambers. A bipolar membrane divides the bMFC into anode and cathode chambers. The bipolar membrane comprises anion and cation exchange layers. The anode chamber side has the cation exchange layer, while the cathode chamber side has the anion exchange layer. The anode chamber of the bMFC was loaded with Shewanella oneidensis MR-1 and lactic acid, while the cathode chamber was loaded with pure water and iron (III) hydroxide. The bMFC generated electrons for 20 days at a maximum current density of 30 mA/m2 and the ohmic resistance value was estimated to be 500 Ω. During the operation of the bMFC, both the anode and cathode chambers kept anaerobic conditions. There was no platinum catalyst in the cathode chamber, which is required for the reaction of protons with oxygen. Therefore, oxygen could not serve as an electron acceptor in the bMFC. We considered a bMFC mechanism in which protons produced by S. oneidensis react with hydroxide ions, the counter anions of Fe3+, inside the bipolar membrane to produce water. In other words, the electron acceptor in bMFC would be Fe3+.

Thermotoga neapolitana.

Like other Thermotogales, Thermotoga neapolitana produces a large quantity of hydrogen using proton as the final electron acceptor. It can utilize a wide range of simple and complex sugars, proteins, and peptides, as well as agricultural and food wastes as carbon and nitrogen sources. Its thermostable enzymes have been used in many industrial settings, such as food processing and consumer products. Biohydrogen gas can power fuel cells, releasing water as the only waste, an extremely appealing prospect in urban transportation.

The relationship between chlorophyll a fluorescence parameters and yield components in sunflower hybrids

The sunflower is considered one of the four most important oilseeds globally. The study was conducted on 16 sunflower hybrids in field conditions to link photosynthesis parameters with yield components using chlorophyll a fluorescence parameters (ChlF), chlorophyll content, leaf temperature and agronomic traits. By analysing the ChlF parameters in the flowering stage of sunflower hybrids, a statistically significant difference was found between the studied hybrids for all the ChlF parameters except for the photosynthetic efficiency index of energy required from exciton to the reduction of ultimate electron acceptors on photosystem I (PItotal). At the same time, the results confirmed the significance of the chlorophyll content, leaf temperature, and agronomic traits for the studied hybrids. The indicators of photosynthetic efficiency showed a significant correlation between the efficiency with which the electron can reduce the final electron acceptors to photosystem I (RE0/ET0), PItotal and plant height. Also, the number of seeds per head showed a positive and very significant correlation with variable fluorescence in step I (VI) and a very highly significant negative correlation with the energy flow which reduces electron end acceptors on the acceptor side of photosystem I (RE0/RC). Using these analyses in sunflower breeding programmes could improve productivity and performance optimisation under changeable growing conditions.

Bacteroides fragilis Maintains Concurrent Capability for Anaerobic and Nanaerobic Respiration.

Bacteroides species can use fumarate and oxygen as terminal electron acceptors during cellular respiration. In the human gut, oxygen diffuses from intestinal epithelial cells supplying "nanaerobic" oxygen levels. Many components of the anaerobic respiratory pathway have been determined, but such analyses have not been performed for nanaerobic respiration. Here, we present genetic, biochemical, enzymatic, and mass spectrometry analyses to elucidate the nanaerobic respiratory pathway in Bacteroides fragilis. Under anaerobic conditions, the transfer of electrons from NADH to the quinone pool has been shown to be contributed by two enzymes, NQR and NDH2. We find that the activity contributed by each under nanaerobic conditions is 77 and 23%, respectively, similar to the activity levels under anaerobic conditions. Using mass spectrometry, we show that the quinone pool also does not differ under these two conditions and consists of a mixture of menaquinone-8 to menaquinone-11, with menaquinone-10 predominant under both conditions. Analysis of fumarate reductase showed that it is synthesized and active under anaerobic and nanaerobic conditions. Previous RNA sequencing data and new transcription reporter assays show that expression of the cytochrome bd oxidase gene does not change under these conditions. Under nanaerobic conditions, we find both increased CydA protein and increased cytochrome bd activity. Reduced-minus-oxidized spectra of membranes showed the presence of heme d when the bacteria were grown in the presence of protoporphyrin IX and iron under both anaerobic and nanaerobic conditions, suggesting that the active oxidase can be assembled with or without oxygen. IMPORTANCE By performing a comprehensive analysis of nanaerobic respiration in Bacteroides fragilis, we show that this organism maintains capabilities for anaerobic respiration on fumarate and nanaerobic respiration on oxygen simultaneously. The contribution of the two NADH:quinone oxidoreductases and the composition of the quinone pool are the same under both conditions. Fumarate reductase and cytochrome bd are both present, and which of these terminal enzymes is active in electron transfer depends on the availability of the final electron acceptor: fumarate or oxygen. The synthesis of cytochrome bd and fumarate reductase under both conditions serves as an adaptation to an environment with low oxygen concentrations so that the bacteria can maximize energy conservation during fluctuating environmental conditions or occupation of different spatial niches.