A genus of gram-negative, anaerobic, rod-shaped bacteria isolated from the bovine RUMEN, the human gingival sulcus, and dental PULPITIS infections.
A family of gram-negative bacteria found primarily in the intestinal tracts and mucous membranes of warm-blooded animals. Its organisms are sometimes pathogenic.
A genus of bacteria found in the reproductive organs, intestinal tract, and oral cavity of animals and man. Some species are pathogenic.
A large group of anaerobic bacteria which show up as pink (negative) when treated by the Gram-staining method.
A subclass of heme a containing cytochromes have a reduced alpha-band absorption of 587-592 nm. They are primarily found in microorganisms.
Dithionite. The dithionous acid ion and its salts.
A group of enzymes that oxidize diverse nitrogenous substances to yield nitrite. (Enzyme Nomenclature, 1992) EC 1.
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
A genus of gram-negative, anaerobic, rod-shaped bacteria. Its organisms are normal inhabitants of the oral, respiratory, intestinal, and urogenital cavities of humans, animals, and insects. Some species may be pathogenic.
The process by which ELECTRONS are transported from a reduced substrate to molecular OXYGEN. (From Bennington, Saunders Dictionary and Encyclopedia of Laboratory Medicine and Technology, 1984, p270)
A flavoprotein containing oxidoreductase that catalyzes the dehydrogenation of SUCCINATE to fumarate. In most eukaryotic organisms this enzyme is a component of mitochondrial electron transport complex II.
A group of substances similar to VITAMIN K 1 which contains a ring of 2-methyl-1,4-naphthoquinione and an isoprenoid side chain of varying number of isoprene units. In vitamin K 2, each isoprene unit contains a double bond. They are produced by bacteria including the normal intestinal flora.
Compounds based on fumaric acid.
A flavoprotein oxidase complex that contains iron-sulfur centers. It catalyzes the oxidation of SUCCINATE to fumarate and couples the reaction to the reduction of UBIQUINONE to ubiquinol.
Oxidoreductases that are specific for the reduction of NITRATES.
The space between the inner and outer membranes of a cell that is shared with the cell wall.
A genus of gram-negative, spiral-shaped bacteria that has been isolated from the intestinal tract of mammals, including humans. It has been associated with PEPTIC ULCER.
Pathological processes involving the PERIODONTIUM including the gum (GINGIVA), the alveolar bone (ALVEOLAR PROCESS), the DENTAL CEMENTUM, and the PERIODONTAL LIGAMENT.

Fused and overlapping rpoB and rpoC genes in Helicobacters, Campylobacters, and related bacteria. (1/59)

The genes coding for the beta (rpoB) and beta' (rpoC) subunits of RNA polymerase are fused in the gastric pathogen Helicobacter pylori but separate in other taxonomic groups. To better understand how the unique fused structure evolved, we determined DNA sequences at and around the rpoB-rpoC junction in 10 gastric and nongastric species of Helicobacter and in members of the related genera Wolinella, Arcobacter, Sulfurospirillum, and Campylobacter. We found the fusion to be specific to Helicobacter and Wolinella genera; rpoB and rpoC overlap in the other genera. The fusion may have arisen by a frameshift mutation at the site of rpoB and rpoC overlap. Loss of good Shine-Dalgarno sequences might then have fixed the fusion in the Helicobacteraceae, even if fusion itself did not confer a selective advantage.  (+info)

The single cysteine residue of the Sud protein is required for its function as a polysulfide-sulfur transferase in Wolinella succinogenes. (2/59)

The periplasmic Sud protein which is induced in Wolinella succinogenes growing by polysulfide respiration, has been previously proposed to serve as a polysulfide binding protein and to transfer polysulfide-sulfur to the active site of polysulfide reductase [Klimmek, O, Kreis, V., Klein, C., Simon, J., Wittershagen, A. & Kroger, A. (1998) Eur. J. Biochem. 253, 263-269.]. The results presented in this communication suggest that polysulfide-sulfur is covalently bound to the single cysteine residue (Cys109) of the Sud monomer, and that Cys109 is required for tight binding of polysulfide-sulfur and for sulfur transfer. A modified Sud protein [(C109S)Sud-His6] in which the cysteine residue was replaced by serine, did not catalyze sulfur transfer from polysulfide to cyanide and did not stimulate electron transport to polysulfide, in contrast to Sud-His6. The polysulfide-sulfur bound to (C109S)Sud-His6 was fully removed upon dialysis against sulfide. After this treatment, Sud-His6 retained one sulfur atom per monomer; thiocyanate was formed upon addition of cyanide to the preparation. After incubation of Sud-His6 with polysulfide, a proportion of the Sud-His6 monomers carried one or two sulfur atoms, as shown by matrix-assisted laser desorption ionization mass spectrometry. The sulfur atoms were absent from monomers derived from Sud-His6 treated with cyanide and from (C109S)Sud-His6 incubated with polysulfide.  (+info)

Progress in understanding structure-function relationships in respiratory chain complex II. (3/59)

Complex II (succinate:quinone oxidoreductase) of aerobic respiratory chains oxidizes succinate to fumarate and passes the electrons directly into the quinone pool. It serves as the only direct link between activity in the citric acid cycle and electron transport in the membrane. Finer details of these reactions and interactions are but poorly understood. However, complex II has extremely similar structural and catalytic properties to quinol:fumarate oxidoreductases of anaerobic organisms, for which X-ray structures have recently become available. These offer new insights into structure-function relationships of this class of flavoenzymes, including evidence favoring protein movement during catalysis.  (+info)

Cytochrome c nitrite reductase from Wolinella succinogenes. Structure at 1.6 A resolution, inhibitor binding, and heme-packing motifs. (4/59)

Cytochrome c nitrite reductase catalyzes the 6-electron reduction of nitrite to ammonia. This second part of the respiratory pathway of nitrate ammonification is a key step in the biological nitrogen cycle. The x-ray structure of the enzyme from the epsilon-proteobacterium Wolinella succinogenes has been solved to a resolution of 1.6 A. It is a pentaheme c-type cytochrome whose heme groups are packed in characteristic motifs that also occur in other multiheme cytochromes. Structures of W. succinogenes nitrite reductase have been obtained with water bound to the active site heme iron as well as complexes with two inhibitors, sulfate and azide, whose binding modes and inhibitory functions differ significantly. Cytochrome c nitrite reductase is part of a highly optimized respiratory system found in a wide range of Gram-negative bacteria. It reduces both anionic and neutral substrates at the distal side of a lysine-coordinated high-spin heme group, which is accessible through two different channels, allowing for a guided flow of reaction educt and product. Based on sequence comparison and secondary structure prediction, we have demonstrated that cytochrome c nitrite reductases constitute a protein family of high structural similarity.  (+info)

Transport of C(4)-dicarboxylates in Wolinella succinogenes. (5/59)

C(4)-dicarboxylate transport is a prerequisite for anaerobic respiration with fumarate in Wolinella succinogenes, since the substrate site of fumarate reductase is oriented towards the cytoplasmic side of the membrane. W. succinogenes was found to transport C(4)-dicarboxylates (fumarate, succinate, malate, and aspartate) across the cytoplasmic membrane by antiport and uniport mechanisms. The electrogenic uniport resulted in dicarboxylate accumulation driven by anaerobic respiration. The molar ratio of internal to external dicarboxylate concentration was up to 10(3). The dicarboxylate antiport was either electrogenic or electroneutral. The electroneutral antiport required the presence of internal Na(+), whereas the electrogenic antiport also operated in the absence of Na(+). In the absence of Na(+), no electrochemical proton potential (delta p) was measured across the membrane of cells catalyzing fumarate respiration. This suggests that the proton potential generated by fumarate respiration is dissipated by the concomitant electrogenic dicarboxylate antiport. Three gene loci (dcuA, dcuB, and dctPQM) encoding putative C(4)-dicarboxylate transporters were identified on the genome of W. succinogenes. The predicted gene products of dcuA and dcuB are similar to the Dcu transporters that are involved in the fumarate respiration of Escherichia coli with external C(4)-dicarboxylates. The genes dctP, -Q, and -M probably encode a binding-protein-dependent secondary uptake transporter for dicarboxylates. A mutant (DcuA(-) DcuB(-)) of W. succinogenes lacking the intact dcuA and dcuB genes grew by nitrate respiration with succinate as the carbon source but did not grow by fumarate respiration with fumarate, malate, or aspartate as substrates. The DcuA(-), DcuB(-), and DctQM(-) mutants grew by fumarate respiration as well as by nitrate respiration with succinate as the carbon source. Cells of the DcuA(-) DcuB(-) mutant performed fumarate respiration without generating a proton potential even in the presence of Na(+). This explains why the DcuA(-) DcuB(-) mutant does not grow by fumarate respiration. Growth by fumarate respiration appears to depend on the function of the Na(+)-dependent, electroneutral dicarboxylate antiport which is catalyzed exclusively by the Dcu transporters. Dicarboxylate transport via the electrogenic uniport is probably catalyzed by the DctPQM transporter and by a fourth, unknown transporter that may also operate as an electrogenic antiporter.  (+info)

Succinate: quinone oxidoreductases: new insights from X-ray crystal structures. (6/59)

Membrane-bound succinate dehydrogenases (succinate:quinone reductases, SQR) and fumarate reductases (quinol:fumarate reductases, QFR) couple the oxidation of succinate to fumarate to the reduction of quinone to quinol and also catalyse the reverse reaction. SQR (respiratory complex II) is involved in aerobic metabolism as part of the citric acid cycle and of the aerobic respiratory chain. QFR is involved in anaerobic respiration with fumarate as the terminal electron acceptor, and is part of an electron transport chain catalysing the oxidation of various donor substrates by fumarate. QFR and SQR complexes are collectively referred to as succinate:quinone oxidoreductases (EC 1.3.5.1), have very similar compositions and are predicted to share similar structures. The complexes consist of two hydrophilic and one or two hydrophobic, membrane-integrated subunits. The larger hydrophilic subunit A carries covalently bound flavin adenine dinucleotide and subunit B contains three iron-sulphur centres. QFR of Wolinella succinogenes and SQR of Bacillus subtilis contain only one hydrophobic subunit (C) with two haem b groups. In contrast, SQR and QFR of Escherichia coli contain two hydrophobic subunits (C and D) which bind either one (SQR) or no haem b group (QFR). The structure of W. succinogenes QFR has been determined at 2.2 A resolution by X-ray crystallography (C.R.D. Lancaster, A. Kroger, M. Auer, H. Michel, Nature 402 (1999) 377-385). Based on this structure of the three protein subunits and the arrangement of the six prosthetic groups, a pathway of electron transfer from the quinol-oxidising dihaem cytochrome b to the site of fumarate reduction and a mechanism of fumarate reduction was proposed. The W. succinogenes QFR structure is different from that of the haem-less QFR of E. coli, described at 3.3 A resolution (T.M. Iverson, C. Luna-Chavez, G. Cecchini, D.C. Rees, Science 284 (1999) 1961-1966), mainly with respect to the structure of the membrane-embedded subunits and the relative orientations of soluble and membrane-embedded subunits. Also, similarities and differences between QFR transmembrane helix IV and transmembrane helix F of bacteriorhodopsin and their implications are discussed.  (+info)

Essential role of Glu-C66 for menaquinol oxidation indicates transmembrane electrochemical potential generation by Wolinella succinogenes fumarate reductase. (7/59)

Quinol:fumarate reductase (QFR) is a membrane protein complex that couples the reduction of fumarate to succinate to the oxidation of quinol to quinone, in a reaction opposite to that catalyzed by the related enzyme succinate:quinone reductase (succinate dehydrogenase). In the previously determined structure of QFR from Wolinella succinogenes, the site of fumarate reduction in the flavoprotein subunit A of the enzyme was identified, but the site of menaquinol oxidation was not. In the crystal structure, the acidic residue Glu-66 of the membrane spanning, diheme-containing subunit C lines a cavity that could be occupied by the substrate menaquinol. Here we describe that, after replacement of Glu-C66 with Gln by site-directed mutagenesis, the resulting mutant is unable to grow on fumarate and the purified enzyme lacks quinol oxidation activity. X-ray crystal structure analysis of the Glu-C66-->Gln variant enzyme at 3.1-A resolution rules out any major structural changes compared with the wild-type enzyme. The oxidation-reduction potentials of the heme groups are not significantly affected. We conclude that Glu-C66 is an essential constituent of the menaquinol oxidation site. Because Glu-C66 is oriented toward a cavity leading to the periplasm, the release of two protons on menaquinol oxidation is expected to occur to the periplasm, whereas the uptake of two protons on fumarate reduction occurs from the cytoplasm. Thus our results indicate that the reaction catalyzed by W. succinogenes QFR generates a transmembrane electrochemical potential.  (+info)

A third crystal form of Wolinella succinogenes quinol:fumarate reductase reveals domain closure at the site of fumarate reduction. (8/59)

Quinol:fumarate reductase (QFR) is a membrane protein complex that couples the reduction of fumarate to succinate to the oxidation of quinol to quinone. Previously, the crystal structure of QFR from Wolinella succinogenes was determined based on two different crystal forms, and the site of fumarate binding in the flavoprotein subunit A of the enzyme was located between the FAD-binding domain and the capping domain [Lancaster, C.R.D., Kroger, A., Auer, M., & Michel, H. (1999) Nature 402, 377--385]. Here we describe the structure of W. succinogenes QFR based on a third crystal form and refined at 3.1 A resolution. Compared with the previous crystal forms, the capping domain is rotated in this structure by approximately 14 degrees relative to the FAD-binding domain. As a consequence, the topology of the dicarboxylate binding site is much more similar to those of membrane-bound and soluble fumarate reductase enzymes from other organisms than to that found in the previous crystal forms of W. succinogenes QFR. This and the effects of the replacement of Arg A301 by Glu or Lys by site-directed mutagenesis strongly support a common mechanism for fumarate reduction in this superfamily of enzymes.  (+info)

I'm sorry for any confusion, but "Wolinella" is not a medical term or a specific condition in human medicine. It is actually the name of a genus of bacteria that are commonly found in the digestive tracts of animals, including humans. These bacteria are named after the Polish microbiologist Michaił Łaszkowski, whose last name was transcribed as "Wolin" in German scientific literature.

The bacteria in this genus are gram-negative, non-spore forming, and can be curved or spiral-shaped. They are often associated with gastrointestinal diseases in animals, but their role in human health and disease is not fully understood. Some research suggests that they may be involved in certain digestive disorders, such as inflammatory bowel disease, but more study is needed to confirm these associations and understand their significance.

Bacteroidaceae is a family of gram-negative, anaerobic or facultatively anaerobic, non-spore forming bacteria that are commonly found in the human gastrointestinal tract. They are rod-shaped and can vary in size and shape. Bacteroidaceae are important breakdowners of complex carbohydrates and proteins in the gut, and play a significant role in maintaining the health and homeostasis of the intestinal microbiota. Some members of this family can also be opportunistic pathogens and have been associated with various infections and diseases, such as abscesses, bacteremia, and periodontal disease.

'Campylobacter' is a genus of gram-negative, spiral-shaped bacteria that are commonly found in the intestinal tracts of animals, including birds and mammals. These bacteria are a leading cause of bacterial foodborne illness worldwide, with Campylobacter jejuni being the most frequently identified species associated with human infection.

Campylobacter infection, also known as campylobacteriosis, typically causes symptoms such as diarrhea (often bloody), abdominal cramps, fever, and vomiting. The infection is usually acquired through the consumption of contaminated food or water, particularly undercooked poultry, raw milk, and contaminated produce. It can also be transmitted through contact with infected animals or their feces.

While most cases of campylobacteriosis are self-limiting and resolve within a week without specific treatment, severe or prolonged infections may require antibiotic therapy. In rare cases, Campylobacter infection can lead to serious complications such as bacteremia (bacterial bloodstream infection), meningitis, or Guillain-Barré syndrome, a neurological disorder that can cause muscle weakness and paralysis.

Preventive measures include proper food handling and cooking techniques, thorough handwashing, and avoiding cross-contamination between raw and cooked foods.

Gram-negative anaerobic bacteria are a type of bacteria that do not require oxygen to grow and are characterized by their cell wall structure, which does not retain crystal violet dye in the Gram staining procedure. This is because they lack a thick peptidoglycan layer in their cell walls, which is typically stained dark purple in Gram-positive bacteria. Instead, gram-negative bacteria have an outer membrane that contains lipopolysaccharides (LPS), which can be toxic to human cells and contribute to the pathogenicity of these organisms.

Examples of gram-negative anaerobic bacteria include Bacteroides fragilis, Prevotella species, and Porphyromonas species. These bacteria are commonly found in the human mouth, gastrointestinal tract, and genitourinary tract, and can cause a variety of infections, including abscesses, wound infections, and bacteremia.

It's important to note that while gram-negative anaerobic bacteria do not require oxygen to grow, some may still tolerate or even prefer oxygen-rich environments. Therefore, the term "anaerobe" can be somewhat misleading when used to describe these organisms.

Cytochrome a1 is a type of cytochrome found in the inner mitochondrial membrane and is a component of the electron transport chain, which plays a crucial role in cellular respiration and energy production. Specifically, cytochrome a1 is involved in the transfer of electrons from cytochrome c to oxygen, the final electron acceptor in the electron transport chain.

Cytochromes are heme-containing proteins that contain a prosthetic group called heme, which consists of an iron atom coordinated to a porphyrin ring. The different types of cytochromes are classified based on the type of heme they contain and their absorption spectra. Cytochrome a1 contains a heme with a formyl group at the 2 position (heme a) and has an alpha band in its absorption spectrum at around 605 nm.

It is worth noting that cytochrome a1 is not always present in all organisms, and its function may vary depending on the species. In some cases, it may be replaced by other types of cytochromes or have additional functions beyond its role in the electron transport chain.

Dithionite is a chemical compound with the formula Na2S2O4. It is also known as sodium hydrosulfite or sodium dithionite. Dithionite is a white crystalline solid that is highly soluble in water and is commonly used as a reducing agent in various industrial and laboratory applications, including the reduction of iron and copper salts, the bleaching of textiles and pulp, and the removal of sulfur dioxide from flue gases.

In medical contexts, dithionite may be used as a reducing agent in some pharmaceutical preparations or as an antidote for certain types of poisoning. However, it is important to note that dithionite can be toxic and corrosive in concentrated forms, and should be handled with care.

Nitrite reductases are a group of enzymes that catalyze the reduction of nitrite (NO2-) to nitric oxide (NO). This reaction is an important part of the nitrogen cycle, particularly in denitrification and dissimilatory nitrate reduction to ammonium (DNRA) processes. Nitrite reductases can be classified into two main types based on their metal co-factors: copper-containing nitrite reductases (CuNiRs) and cytochrome cd1 nitrite reductases. CuNiRs are typically found in bacteria and fungi, while cytochrome cd1 nitrite reductases are primarily found in bacteria. These enzymes play a crucial role in the global nitrogen cycle and have potential implications for environmental and medical research.

Oxidoreductases are a class of enzymes that catalyze oxidation-reduction reactions, which involve the transfer of electrons from one molecule (the reductant) to another (the oxidant). These enzymes play a crucial role in various biological processes, including energy production, metabolism, and detoxification.

The oxidoreductase-catalyzed reaction typically involves the donation of electrons from a reducing agent (donor) to an oxidizing agent (acceptor), often through the transfer of hydrogen atoms or hydride ions. The enzyme itself does not undergo any permanent chemical change during this process, but rather acts as a catalyst to lower the activation energy required for the reaction to occur.

Oxidoreductases are classified and named based on the type of electron donor or acceptor involved in the reaction. For example, oxidoreductases that act on the CH-OH group of donors are called dehydrogenases, while those that act on the aldehyde or ketone groups are called oxidases. Other examples include reductases, peroxidases, and catalases.

Understanding the function and regulation of oxidoreductases is important for understanding various physiological processes and developing therapeutic strategies for diseases associated with impaired redox homeostasis, such as cancer, neurodegenerative disorders, and cardiovascular disease.

Bacteroides are a genus of gram-negative, anaerobic, rod-shaped bacteria that are normally present in the human gastrointestinal tract. They are part of the normal gut microbiota and play an important role in breaking down complex carbohydrates and other substances in the gut. However, some species of Bacteroides can cause opportunistic infections, particularly in individuals with weakened immune systems or when they spread to other parts of the body. They are resistant to many commonly used antibiotics, making infections caused by these bacteria difficult to treat.

The Electron Transport Chain (ETC) is a series of complexes in the inner mitochondrial membrane that are involved in the process of cellular respiration. It is the final pathway for electrons derived from the oxidation of nutrients such as glucose, fatty acids, and amino acids to be transferred to molecular oxygen. This transfer of electrons drives the generation of a proton gradient across the inner mitochondrial membrane, which is then used by ATP synthase to produce ATP, the main energy currency of the cell.

The electron transport chain consists of four complexes (I-IV) and two mobile electron carriers (ubiquinone and cytochrome c). Electrons from NADH and FADH2 are transferred to Complex I and Complex II respectively, which then pass them along to ubiquinone. Ubiquinone then transfers the electrons to Complex III, which passes them on to cytochrome c. Finally, cytochrome c transfers the electrons to Complex IV, where they combine with oxygen and protons to form water.

The transfer of electrons through the ETC is accompanied by the pumping of protons from the mitochondrial matrix to the intermembrane space, creating a proton gradient. The flow of protons back across the inner membrane through ATP synthase drives the synthesis of ATP from ADP and inorganic phosphate.

Overall, the electron transport chain is a crucial process for generating energy in the form of ATP in the cell, and it plays a key role in many metabolic pathways.

Succinate dehydrogenase (SDH) is an enzyme complex that plays a crucial role in the process of cellular respiration, specifically in the citric acid cycle (also known as the Krebs cycle) and the electron transport chain. It is located in the inner mitochondrial membrane of eukaryotic cells.

SDH catalyzes the oxidation of succinate to fumarate, converting it into a molecule of fadaquate in the process. During this reaction, two electrons are transferred from succinate to the FAD cofactor within the SDH enzyme complex, reducing it to FADH2. These electrons are then passed on to ubiquinone (CoQ), which is a mobile electron carrier in the electron transport chain, leading to the generation of ATP, the main energy currency of the cell.

SDH is also known as mitochondrial complex II because it is the second complex in the electron transport chain. Mutations in the genes encoding SDH subunits or associated proteins have been linked to various human diseases, including hereditary paragangliomas, pheochromocytomas, gastrointestinal stromal tumors (GISTs), and some forms of neurodegenerative disorders.

Vitamin K2, also known as menaquinone, is a fat-soluble vitamin that plays a crucial role in the blood clotting process and bone metabolism. It is one of the two main forms of Vitamin K (the other being Vitamin K1 or phylloquinone), and it is found in animal-based foods and fermented foods.

Vitamin K2 is a collective name for a group of vitamin K compounds characterized by the presence of a long-chain fatty acid attached to the molecule. The most common forms of Vitamin K2 are MK-4 and MK-7, which differ in the length of their side chains.

Vitamin K2 is absorbed more efficiently than Vitamin K1 and has a longer half-life, which means it stays in the body for a longer period. It is stored in various tissues, including bones, where it plays an essential role in maintaining bone health by assisting in the regulation of calcium deposition and helping to prevent the calcification of blood vessels and other soft tissues.

Deficiency in Vitamin K2 is rare but can lead to bleeding disorders and weakened bones. Food sources of Vitamin K2 include animal-based foods such as liver, egg yolks, and fermented dairy products like cheese and natto (a Japanese food made from fermented soybeans). Some studies suggest that supplementing with Vitamin K2 may have benefits for bone health, heart health, and cognitive function. However, more research is needed to confirm these potential benefits.

Fumarates are the salts or esters of fumaric acid, a naturally occurring organic compound with the formula HO2C-CH=CH-CO2H. In the context of medical therapy, fumarates are used as medications for the treatment of psoriasis and multiple sclerosis.

One such medication is dimethyl fumarate (DMF), which is a stable salt of fumaric acid. DMF has anti-inflammatory and immunomodulatory properties, and it's used to treat relapsing forms of multiple sclerosis (MS) and moderate-to-severe plaque psoriasis.

The exact mechanism of action of fumarates in these conditions is not fully understood, but they are thought to modulate the immune system and have antioxidant effects. Common side effects of fumarate therapy include gastrointestinal symptoms such as diarrhea, nausea, and abdominal pain, as well as flushing and skin reactions.

Electron Transport Complex II, also known as succinate-Q oxidoreductase, is a key component of the electron transport chain in the inner mitochondrial membrane. It plays a crucial role in the process of cellular respiration, where it facilitates the transfer of electrons from succinate to ubiquinone (Q), thereby generating a proton gradient across the membrane. This gradient drives the synthesis of ATP, which is the primary source of energy for the cell.

The complex is composed of four core subunits: flavoprotein (Fp), iron-sulfur protein (Ip), cytochrome b (Cyb), and ubiquinone-binding protein (Qp). Electrons from succinate are accepted by FAD in the Fp subunit, and then transferred to the Ip subunit containing iron-sulfur clusters. From there, the electrons are moved to heme groups in the Cyb subunit, and finally passed on to ubiquinone at the Qp subunit.

In addition to its role in the electron transport chain, Complex II has been implicated in various cellular processes such as regulation of reactive oxygen species (ROS) production and modulation of apoptosis. Mutations in genes encoding Complex II subunits have been associated with several human diseases, including neurodegenerative disorders and cancer.

Nitrate reductases are a group of enzymes that catalyze the reduction of nitrate (NO3-) to nitrite (NO2-). This process is an essential part of the nitrogen cycle, where nitrate serves as a terminal electron acceptor in anaerobic respiration for many bacteria and archaea. In plants, this enzyme plays a crucial role in nitrogen assimilation by reducing nitrate to ammonium (NH4+), which can then be incorporated into organic compounds. Nitrate reductases require various cofactors, such as molybdenum, heme, and/or FAD, for their activity. There are three main types of nitrate reductases: membrane-bound (which use menaquinol as an electron donor), cytoplasmic (which use NADH or NADPH as an electron donor), and assimilatory (which also use NADH or NADPH as an electron donor).

The periplasm is a term used in the field of microbiology, specifically in reference to gram-negative bacteria. It refers to the compartment or region located between the bacterial cell's inner membrane (cytoplasmic membrane) and its outer membrane. This space contains a unique mixture of proteins, ions, and other molecules that play crucial roles in various cellular processes, such as nutrient uptake, waste excretion, and the maintenance of cell shape.

The periplasm is characterized by its peptidoglycan layer, which provides structural support to the bacterial cell and protects it from external pressures. This layer is thinner in gram-negative bacteria compared to gram-positive bacteria, which do not have an outer membrane and thus lack a periplasmic space.

Understanding the periplasmic region of gram-negative bacteria is essential for developing antibiotics and other therapeutic agents that can target specific cellular processes or disrupt bacterial growth and survival.

"Helicobacter" is a genus of gram-negative, spiral-shaped bacteria that are commonly found in the stomach. The most well-known species is "Helicobacter pylori," which is known to cause various gastrointestinal diseases, such as gastritis, peptic ulcers, and gastric cancer. These bacteria are able to survive in the harsh acidic environment of the stomach by producing urease, an enzyme that neutralizes stomach acid. Infection with "Helicobacter pylori" is usually acquired in childhood and can persist for life if not treated.

According to the American Academy of Periodontology, periodontal diseases are chronic inflammatory conditions that affect the tissues surrounding and supporting the teeth. These tissues include the gums, periodontal ligament, and alveolar bone. The primary cause of periodontal disease is bacterial plaque, a sticky film that constantly forms on our teeth.

There are two major stages of periodontal disease:

1. Gingivitis: This is the milder form of periodontal disease, characterized by inflammation of the gums (gingiva) without loss of attachment to the teeth. The gums may appear red, swollen, and bleed easily during brushing or flossing. At this stage, the damage can be reversed with proper dental care and improved oral hygiene.
2. Periodontitis: If left untreated, gingivitis can progress to periodontitis, a more severe form of periodontal disease. In periodontitis, the inflammation extends beyond the gums and affects the deeper periodontal tissues, leading to loss of bone support around the teeth. Pockets filled with infection-causing bacteria form between the teeth and gums, causing further damage and potential tooth loss if not treated promptly.

Risk factors for developing periodontal disease include poor oral hygiene, smoking or using smokeless tobacco, genetic predisposition, diabetes, hormonal changes (such as pregnancy or menopause), certain medications, and systemic diseases like AIDS or cancer. Regular dental check-ups and good oral hygiene practices are crucial for preventing periodontal disease and maintaining overall oral health.

Parte, A. C. "Wolinella". LPSN. taxonomy. "Taxonomy browser (Wolinella succinogenes DSM 1740)". www.ncbi.nlm.nih.gov. Retrieved ... "Wolinella Tanner et al., 1981 - Checklist View". www.gbif.org. Retrieved 2016-04-16. taxonomy. "Taxonomy browser (Wolinella)". ... The only publicly available strain of Wolinella is Wolinella succinogenes DSM 1740 (ATCC 29543). The original isolation of this ... Strains of Wolinella have been isolated from feline and canine oral cavities. Only one strain is currently published with ...
nov., Wolinella succinogenes (Vibrio succinogenes Wolin et al.) comb. nov., and Description of Bacteroides gracilis sp. nov., ... Tanner, A. C. R.; Badger, S.; Lai, C.-H; Listgarten, M. A.; Visconti, R. A.; Socransky, S. S. (1981). "Wolinella gen. ... Wolinella recta sp. nov., Campylobacter concisus sp. nov., and Eikenella corrodens from Humans with Periodontal Disease". ...
Wolinella africanus" Bohr et al. 2003 "Ca. Xenohaliotis californiensis" Friedman et al. 2000 "Ca. Xiphinematobacter americani" ...
Publicly know is one species, Wolinella succinogenens. Wolinella succinogenens is a well known non-vent sulfur-reducing ... Wolinella is a sulfur reducing genus of bacteria and incomplete oxidizer that cannot use acetate as an electron donor. ... for instance the genera Wolinella, Ammonifex, Desulfuromonas and Desulfurobacterium. On the other side, there are obligate ...
Ullmann R, Gross R, Simon J, Unden G, Kroger A (October 2000). "Transport of C(4)-dicarboxylates in Wolinella succinogenes". J ...
2003). "Complete genome sequence and analysis of Wolinella succinogenes". Proc. Natl. Acad. Sci. U.S.A. 100 (20): 11690-5. ...
1992). "The quinone-reactive Ni/Fe-hydrogenase of Wolinella succinogenes". Eur. J. Biochem. 206 (1): 93-102. doi:10.1111/j.1432 ... 1993). "The quinone-reactive Ni/Fe-hydrogenase of Wolinella Succinogenes". Eur. J. Biochem. 214 (3): 949-50. doi:10.1111/j.1432 ... Gross R, Simon J, Lancaster CR, Kröger A (1998). "Identification of histidine residues in Wolinella succinogenes hydrogenase ...
Lancaster CR, Kröger A, Auer M, Michel H (November 1999). "Structure of fumarate reductase from Wolinella succinogenes at 2.2 A ... fumarate reductase has also been studied in other organisms including Wolinella succinogenes, Helicobacter pylori, and ...
Most of the known species inhabit the digestive tracts of animals and serve as symbionts (Wolinella spp. in cattle) or ... The Campylobacterota consist of few known genera, mainly the curved to spirilloid Wolinella spp., Helicobacter spp., and ...
It was shown in 1973 that this process occurs between Ruminococcus albus and Wolinella succinogenes. A more recent publication ...
... and Wolinella taxonomy: emendation of generic descriptions and proposal of Arcobacter gen-nov". International Journal of ...
... and Wolinella Taxonomy: Emendation of Generic Descriptions and Proposal of Arcobacter gen. nov". International Journal of ...
1991). "Revision of Campylobacter, Helicobacter, and Wolinella taxonomy: emendation of generic descriptions and proposal of ...
... is the mediator between the quinone pool and the cytochrome c nitrite reductase of Wolinella succinogenes". Molecular ...
... involving the genus Ruminococcus is a paper describing interspecies hydrogen transfer between Ruminococcus albus and Wolinella ...
These bacteria are nutritionally fastidious and physiologically similar to other Helicobacter species and Wolinella ...
Wolinella (with H 2 as reducing equivalent donor), some Knallgas-bacteria, some sulfate-reducing bacteria[citation needed] ...
Staphylococcus aerogenes Staphylococcus aureus Streptococcus agalactiae Streptococcus faecalis Streptococcus mutans Wolinella ...
... an American bacteriologist Wolinella - M. J. Wolin, an American bacteriologist Annwoodia - Ann P. Wood, a British ...
Volgia Volnovachia Volviflustrellaria Voorthuyseniella Wassypora Watersipora Wawalia Wilbertopora Wjatkella Wolinella Woodipora ...
Wolinella MeSH B03.440.450.009 - Actinobacillus MeSH B03.440.450.009.050 - Actinobacillus actinomycetemcomitans MeSH B03.440. ... Wolinella MeSH B03.660.250.015 - Acidithiobacillus MeSH B03.660.250.015.800 - Acidithiobacillus thiooxidans MeSH B03.660. ...
Parte, A. C. "Wolinella". LPSN. taxonomy. "Taxonomy browser (Wolinella succinogenes DSM 1740)". www.ncbi.nlm.nih.gov. Retrieved ... "Wolinella Tanner et al., 1981 - Checklist View". www.gbif.org. Retrieved 2016-04-16. taxonomy. "Taxonomy browser (Wolinella)". ... The only publicly available strain of Wolinella is Wolinella succinogenes DSM 1740 (ATCC 29543). The original isolation of this ... Strains of Wolinella have been isolated from feline and canine oral cavities. Only one strain is currently published with ...
BRENDA - The Comprehensive Enzyme Information System
WOLINELLA SUCCINOGENES L-ASPARAGINASE S121 + L-GLUTAMIC ACID - 5K4H , canSARS ...
Because many animal bites are never reported, determining the exact incidence of bite wounds in the United States, let alone the world, is difficult. In 2012, there were approximately 70 million pet dogs and 74 million pet cats in the US.
nov., Wolinella recta sp. nov., Campylobacter concisus sp. nov., and Eikenella corrodens from Humans with Periodontal Disease. ... C. curvus (previously named as Wolinella curva) was first described in 1984 by Tanner et al. (Tanner et al., 1984). C. curvus ... Tanner, A., Listgarten, M., and Ebersole, J. (1984). Wolinella curva sp. nov.:"Vibrio succinogenes" of human origin. Int. J. ... 1993). Antigenic properties of Campylobacter rectus (Wolinella recta) major S-layer proteins. FEMS Microbiol. Lett. 108, 275- ...
The Campylobacter/Wolinella cluster is not specifically includable in either the alpha, beta or gamma subdivisions of the ... In terms of overall position in bacterial phylogeny, the Campylobacter/Wolinella cluster represents a deep branching most ... jejuni and Wolinella succinogenes. In addition limited partial sequence data were obtained from the 16S rRNAs of isolates of C ... The Campylobacter/Wolinella cluster is not specifically includable in either the alpha, beta or gamma subdivisions of the ...
M. Kern and J. Simon, "Characterization of the NapGH quinol dehydrogenase complex involved in Wolinella succinogenes nitrate ...
Wolinella RSV_genus1140 Bacteria;Proteobacteria;Epsilonproteobacteria;Campylobacterales;NA;NA RSV_genus1141 Bacteria; ...
Ohta H., Gottschal J. C., Fukui K., Kato K. 1991; Aspartate and asparagine as electron acceptors for Wolinella recta . Oral ...
Wolinella Faecalibacterium - Preferred Concept UI. M000608920. Scope note. A genus of Gram-negative, non-spore forming, ...
Identification and Prevalence of Helicobacter Pylori Virulence Genes Baba and Caga in Wolinella Isolates from the Oral Cavity ... Wolinella spp. and Helicobacter spp. have been repeatedly reported in the oral cavity of dogs and are associated with ... No cagA and babA genes were detected in the Wolinella spp. or non-pylori Helicobacter genomes. Our results confirmed that ... The species-specific 16s rRNA genes from the Helicobacter and Wolinella genera were detected in 58.06% and 83.87% of the oral ...
Wolinella succinogenes periplasmic sulfide dehydrogenase (sud). Sud has been characterized as a polysulfide:cyanide ...
... and a Wolinella spp.) were positive for cpa and only one was positive for cpb. The netB gene was present in only two (4%) of ...
Wolinella succinogenes use Wolinella Woodfordia Wrightia antidysenterica use Kurchi Wu wei zi use Schisandra ...
Wolinella Wolinella succinogenes use Wolinella Woodfordia World Wide Web use Internet Wortmanina ...
Wolinella succinogenes use Wolinella Woodfordia Wrightia antidysenterica use Kurchi Wu wei zi use Schisandra ...
Wolinella succinogenes use Wolinella Woodfordia Wrightia antidysenterica use Kurchi Wu wei zi use Schisandra ...
Wolinella succinogenes use Wolinella Woodfordia Workflow use Fluxo de Trabalho Workshops use Educação ...
Wolinella succinogenes use Wolinella Woodfordia Wrightia antidysenterica use Kurchi Wu wei zi use Schisandra ...
Wolinella succinogenes use Wolinella Woodfordia Wrightia antidysenterica use Kurchi Wu wei zi use Schisandra ...
Wolinella succinogenes use Wolinella Woodfordia Wrightia antidysenterica use Kurchi Wu wei zi use Schisandra ...
Wolinella succinogenes use Wolinella Woodfordia Wrightia antidysenterica use Kurchi Wu wei zi use Schisandra ...
Wolinella succinogenes use Wolinella Woodfordia Workflow use Fluxo de Trabalho Workshops use Educação ...
Wolinella succinogenes use Wolinella Woodfordia Wrightia antidysenterica use Kurchi Wu wei zi use Schisandra ...
Wolinella succinogenes use Wolinella Woodfordia Wrightia antidysenterica use Kurchi Wu wei zi use Schisandra ...
Wolinella. A genus of gram-negative, anaerobic, rod-shaped bacteria isolated from the bovine RUMEN, the human gingival sulcus, ... AlcaligenesAlcaligenes faecalisBacteroidaceaeParacoccusNitrosomonas europaeaParacoccus pantotrophusWolinella ... Nitrous OxideMolecular Sequence DataNADPH-Ferrihemoprotein ReductaseFerredoxinsFerredoxin-NADP ReductaseHydroxylamineWolinella ...
Wolinella recta Active Synonym false false Associated Value Sets Value Set Name Version(s) ...
  • The only publicly available strain of Wolinella is Wolinella succinogenes DSM 1740 (ATCC 29543). (wikipedia.org)
  • A complete 5S rRNA sequence was determined for two strains of Campylobacter jejuni and extensive partial sequences of the 16S rRNA were obtained for several strains of C. jejuni and Wolinella succinogenes. (nasa.gov)
  • In terms of overall position in bacterial phylogeny, the Campylobacter/Wolinella cluster represents a deep branching most probably located within an expanded version of the Division containing the purple photosynthetic bacteria and their relatives. (nasa.gov)
  • The Campylobacter/Wolinella cluster is not specifically includable in either the alpha, beta or gamma subdivisions of the purple bacteria. (nasa.gov)
  • Campylobacter, Arcobacter, Helicobacter and Wolinella spp. (canada.ca)
  • The genus Wolinella is a member of the Campylobacterales order of Bacteria. (wikipedia.org)
  • Strains of Wolinella have been isolated from feline and canine oral cavities. (wikipedia.org)
  • Results showed that all isolates but 3 from poultry litter (which were determined to be C. bifermentans, Bacteroides caccae, and a Wolinella spp. (auburn.edu)
  • Some of the research done on Wolinella succinogenes includes its mutualistic relationship with hydrogen-producing organisms, including Ruminococcus albus. (wikipedia.org)
  • The only publicly available strain of Wolinella is Wolinella succinogenes DSM 1740 (ATCC 29543). (wikipedia.org)
  • This bacterium was originally classified as Vibrio succinogenes, but was reclassified in 1981 to Wolinella succinogenes by A. C. R. Tanner et al. (wikipedia.org)
  • Some of the research done on Wolinella succinogenes includes its mutualistic relationship with hydrogen-producing organisms, including Ruminococcus albus. (wikipedia.org)
  • Wolinella succinogenes molecular hydrogen using a fumarate reductase, producing succinate. (wikipedia.org)
  • strain, and a Wolinella succinogenes strain or 3H- or 14C-labeled 23S rRNAs from 13 gram-negative reference strains. (nih.gov)
  • Untersuchungen zum N2O-Metabolismus des Nitrat-ammonifizierenden Bakteriums Wolinella succinogenes. (tu-darmstadt.de)
  • Complete genome sequence and analysis of Wolinella succinogenes. (tu-darmstadt.de)
  • From the combined mutant data and structural information derived from Escherichia coli and Wolinella succinogenes quinol:fumarate reductase, we suggest that carboxin acts by blocking binding of ubiquinone to the active site. (bvsalud.org)
  • Only one strain is currently published with Candidatus status: Candidatus Wolinella africanus. (wikipedia.org)