A report on Flavin adenine dinucleotide

Reaction of FAD to form FADH2
Approximate absorption spectrum for FAD
Mechanism 1. Hydride transfer occurs by addition of H+ and 2 e−
Mechanism 2. Hydride transfer by abstraction of hydride from NADH
Mechanism 3. Radical formation by electron abstraction
Mechanism 4. The loss of hydride to electron deficient R group
Mechanism 5. Use of nucleophilic addition to break R1-R2 bond
Mechanism 6. Carbon radical reacts with O2 and acid to form H2O2
Riboflavin
FADH{{sub|2}}

Redox-active coenzyme associated with various proteins, which is involved with several enzymatic reactions in metabolism.

- Flavin adenine dinucleotide
Reaction of FAD to form FADH2

29 related topics with Alpha

Overall
The electron transport chain in the cell is the site of oxidative phosphorylation. The NADH and succinate generated in the citric acid cycle are oxidized, releasing the energy of O2 to power the ATP synthase.

Oxidative phosphorylation

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Metabolic pathway in which cells use enzymes to oxidize nutrients, thereby releasing chemical energy in order to produce adenosine triphosphate (ATP).

Metabolic pathway in which cells use enzymes to oxidize nutrients, thereby releasing chemical energy in order to produce adenosine triphosphate (ATP).

The electron transport chain in the cell is the site of oxidative phosphorylation. The NADH and succinate generated in the citric acid cycle are oxidized, releasing the energy of O2 to power the ATP synthase.
Reduction of coenzyme Q from its ubiquinone form (Q) to the reduced ubiquinol form (QH2).
Complex I or NADH-Q oxidoreductase. The abbreviations are discussed in the text. In all diagrams of respiratory complexes in this article, the matrix is at the bottom, with the intermembrane space above.
Complex II: Succinate-Q oxidoreductase.
The two electron transfer steps in complex III: Q-cytochrome c oxidoreductase. After each step, Q (in the upper part of the figure) leaves the enzyme.
Complex IV: cytochrome c oxidase.
Mechanism of ATP synthase. ATP is shown in red, ADP and phosphate in pink and the rotating γ subunit in black.

The energy stored in the chemical bonds of glucose is released by the cell in the citric acid cycle producing carbon dioxide, and the energetic electron donors NADH and FADH.

the fmn binding protein athal3

Flavoprotein

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Flavoproteins are proteins that contain a nucleic acid derivative of riboflavin.

Flavoproteins are proteins that contain a nucleic acid derivative of riboflavin.

the fmn binding protein athal3

Flavoproteins have either FMN or FAD (flavin adenine dinucleotide) as a prosthetic group or as a cofactor.

This nucleotide contains the five-carbon sugar deoxyribose (at center), a nucleobase called adenine (upper right), and one phosphate group (left). The deoxyribose sugar joined only to the nitrogenous base forms a <u title="Nucleotide">Deoxyribonucleoside called deoxyadenosine, whereas the whole structure along with the phosphate group is a <u title="Deoxyadenosine monophosphate" href="deoxyadenosine monophosphate">nucleotide, a constituent of DNA with the name deoxyadenosine monophosphate.

Nucleotide

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Nucleotides are organic molecules consisting of a nucleoside and a phosphate.

Nucleotides are organic molecules consisting of a nucleoside and a phosphate.

This nucleotide contains the five-carbon sugar deoxyribose (at center), a nucleobase called adenine (upper right), and one phosphate group (left). The deoxyribose sugar joined only to the nitrogenous base forms a <u title="Nucleotide">Deoxyribonucleoside called deoxyadenosine, whereas the whole structure along with the phosphate group is a <u title="Deoxyadenosine monophosphate" href="deoxyadenosine monophosphate">nucleotide, a constituent of DNA with the name deoxyadenosine monophosphate.
Showing the arrangement of nucleotides within the structure of nucleic acids: At lower left, a monophosphate nucleotide; its nitrogenous base represents one side of a base-pair. At the upper right, four nucleotides form two base-pairs: thymine and adenine (connected by double hydrogen bonds) and guanine and cytosine (connected by triple hydrogen bonds). The individual nucleotide monomers are chain-joined at their sugar and phosphate molecules, forming two 'backbones' (a double helix) of nucleic acid, shown at upper left.
Structural elements of three nucleo tides —where one-, two- or three-phosphates are attached to the nucleo side (in yellow, blue, green) at center: 1st, the nucleotide termed as a nucleoside mono phosphate is formed by adding a phosphate (in red); 2nd, adding a second phosphate forms a nucleoside di phosphate; 3rd, adding a third phosphate results in a nucleoside tri phosphate. + The nitrogenous base (nucleobase) is indicated by "Base" and "glycosidic bond" (sugar bond). All five primary, or canonical, bases—the purines and pyrimidines—are sketched at right (in blue).
The synthesis of UMP. The color scheme is as follows: enzymes, <span style="color: rgb(219,155,36);">coenzymes, <span style="color: rgb(151,149,45);">substrate names , <span style="color: rgb(128,0,0);">inorganic molecules
The synthesis of IMP. The color scheme is as follows: enzymes, <span style="color: rgb(219,155,36);">coenzymes, <span style="color: rgb(151,149,45);">substrate names , <span style="color: rgb(227,13,196);">metal ions , <span style="color: rgb(128,0,0);">inorganic molecules

They provide chemical energy—in the form of the nucleoside triphosphates, adenosine triphosphate (ATP), guanosine triphosphate (GTP), cytidine triphosphate (CTP) and uridine triphosphate (UTP)—throughout the cell for the many cellular functions that demand energy, including: amino acid, protein and cell membrane synthesis, moving the cell and cell parts (both internally and intercellularly), cell division, etc. In addition, nucleotides participate in cell signaling (cyclic guanosine monophosphate or cGMP and cyclic adenosine monophosphate or cAMP), and are incorporated into important cofactors of enzymatic reactions (e.g. coenzyme A, FAD, FMN, NAD, and NADP+).

Pyruvate dehydrogenase complex

Pyruvate dehydrogenase complex

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Complex of three enzymes that converts pyruvate into acetyl-CoA by a process called pyruvate decarboxylation.

Complex of three enzymes that converts pyruvate into acetyl-CoA by a process called pyruvate decarboxylation.

Pyruvate dehydrogenase complex
Pymol-generated image of E1 subunit of pyruvate dehydrogenase complex in E. Coli
Pymol-generated E3 subunit of pyruvate dehydrogenase complex in Pseudomonas putida
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First, FAD oxidizes dihydrolipoate back to its lipoate resting state, producing FADH2.

Gerty Cori and Carl Cori jointly won the Nobel Prize in 1947 for their discovery of the Cori cycle at RPMI.

Biochemistry

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Study of chemical processes within and relating to living organisms.

Study of chemical processes within and relating to living organisms.

Gerty Cori and Carl Cori jointly won the Nobel Prize in 1947 for their discovery of the Cori cycle at RPMI.
DNA structure
The main elements that compose the human body shown from most abundant (by mass) to least abundant.
Structures of some common lipids. At the top are cholesterol and oleic acid. The middle structure is a triglyceride composed of oleoyl, stearoyl, and palmitoyl chains attached to a glycerol backbone. At the bottom is the common phospholipid, phosphatidylcholine.
The general structure of an α-amino acid, with the amino group on the left and the carboxyl group on the right.
Generic amino acids (1) in neutral form, (2) as they exist physiologically, and (3) joined together as a dipeptide.
A schematic of hemoglobin. The red and blue ribbons represent the protein globin; the green structures are the heme groups.
Examples of protein structures from the Protein Data Bank
Members of a protein family, as represented by the structures of the isomerase domains
The structure of deoxyribonucleic acid (DNA), the picture shows the monomers being put together.
Structural elements of common nucleic acid constituents. Because they contain at least one phosphate group, the compounds marked nucleoside monophosphate, nucleoside diphosphate and nucleoside triphosphate are all nucleotides (not simply phosphate-lacking nucleosides).
Schematic relationship between biochemistry, genetics, and molecular biology.

The two molecules acetyl-CoA (from one molecule of glucose) then enter the citric acid cycle, producing two molecules of ATP, six more NADH molecules and two reduced (ubi)quinones (via FADH2 as enzyme-bound cofactor), and releasing the remaining carbon atoms as carbon dioxide.

hDAAO head-to-head connection

D-amino acid oxidase

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Enzyme with the function on a molecular level to oxidize D-amino acids to the corresponding α-keto acids, producing ammonia and hydrogen peroxide.

Enzyme with the function on a molecular level to oxidize D-amino acids to the corresponding α-keto acids, producing ammonia and hydrogen peroxide.

hDAAO head-to-head connection
SchizophreniaBrain

It is also considered a peroxisomal enzyme containing FAD as a cofactor.

Schematic demonstrating mitochondrial fatty acid beta-oxidation and effects of long-chain 3-hydroxyacyl-coenzyme A dehydrogenase deficiency, LCHAD deficiency

Beta oxidation

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Schematic demonstrating mitochondrial fatty acid beta-oxidation and effects of long-chain 3-hydroxyacyl-coenzyme A dehydrogenase deficiency, LCHAD deficiency
Complete beta oxidation of linoleic acid (an unsaturated fatty acid).

In biochemistry and metabolism, beta-oxidation is the catabolic process by which fatty acid molecules are broken down in the cytosol in prokaryotes and in the mitochondria in eukaryotes to generate acetyl-CoA, which enters the citric acid cycle, and NADH and FADH2, which are co-enzymes used in the electron transport chain.

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Acyl-CoA dehydrogenase

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Acyl-CoA dehydrogenases (ACADs) are a class of enzymes that function to catalyze the initial step in each cycle of fatty acid β-oxidation in the mitochondria of cells.

Acyl-CoA dehydrogenases (ACADs) are a class of enzymes that function to catalyze the initial step in each cycle of fatty acid β-oxidation in the mitochondria of cells.

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Structure of the medium-chain acyl-CoA dehydrogenase tetramer. FAD molecules are shown in yellow. PDB code: 1egc.
The overall mechanism of Acyl-CoA dehydrogenase.
Close-up of the medium-chain acyl-CoA dehydrogenase active site. FAD is bound. The substrate will bind in the space between Glu-376 and FAD when fatty acid oxidation is initialized. PDB code: 3mdd.

Flavin adenine dinucleotide (FAD) is a required co-factor in addition to the presence of an active site glutamate in order for the enzyme to function.

Biological roles of succinate. Inside the mitochondria, succinate serves as an intermediate in multiple metabolic pathways and contributes to the generation of ROS. Outside the mitochondria, succinate functions as both an intracellular and extracellular signaling molecule. OOA=oxaloacetate; a-KG=alpha ketoglutarate; GLUT= Glutamate; GABA = gamma-aminobutyric acid; SSA=Succinic semialdehyde ; PHD= prolyl hydroxylase; HIF-1a=hypoxia inducible factor 1a; TET= Ten-eleven Translocation Enzymes; JMJD3= Histone demethylase Jumonji D3

Succinic acid

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Dicarboxylic acid with the chemical formula 2(CO2H)2.

Dicarboxylic acid with the chemical formula 2(CO2H)2.

Biological roles of succinate. Inside the mitochondria, succinate serves as an intermediate in multiple metabolic pathways and contributes to the generation of ROS. Outside the mitochondria, succinate functions as both an intracellular and extracellular signaling molecule. OOA=oxaloacetate; a-KG=alpha ketoglutarate; GLUT= Glutamate; GABA = gamma-aminobutyric acid; SSA=Succinic semialdehyde ; PHD= prolyl hydroxylase; HIF-1a=hypoxia inducible factor 1a; TET= Ten-eleven Translocation Enzymes; JMJD3= Histone demethylase Jumonji D3
Amino acid sequence of GPR91. Succinate binds to GPR91, a 7-transmembrane G-protein coupled receptor, located on a variety of cell types. Red amino acids represent those involved in binding succinate. All other amino acids are colored according to their chemical properties (grey=nonpolar, cyan=negative charge, dark blue = positive charge, green=aromatic, dark purple=polar and noncharged, orange/light purple = special cases).
Accumulated succinate inhibits dioxygenases, such as histone and DNA demethylases or prolyl hydroxylases, by competitive inhibition. Thus, succinate modifies the epigenic landscape and regulates gene expression.

This enzyme complex is a 4 subunit membrane-bound lipoprotein which couples the oxidation of succinate to the reduction of ubiquinone via the intermediate electron carriers FAD and three 2Fe-2S clusters.

L-Ribose Fischer Projection

Ribose

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Simple sugar and carbohydrate with molecular formula C5H10O5 and the linear-form composition H−−(CHOH)4−H.

Simple sugar and carbohydrate with molecular formula C5H10O5 and the linear-form composition H−−(CHOH)4−H.

L-Ribose Fischer Projection
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Pentose Phosphate Pathway: begins with -glucose and includes -ribose 5-phosphate as an intermediate
α-{{sm|d}}-Ribopyranose
β-{{sm|d}}-Ribopyranose
α-{{sm|d}}-Ribofuranose
β-{{sm|d}}-Ribofuranose
2' endo
2' endo 3' exo
3' endo 2' exo
3' endo

For example, nicotinamide adenine dinucleotide (NAD), flavin adenine dinucleotide (FAD), and nicotinamide adenine dinucleotide phosphate (NADP) all contain the -ribofuranose moiety.