Information about Nitrate Reductase
Nitrate reductase enzymes are a group of enzymes which reduce nitrate to nitrite.
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- Nitrate reductase (1)- is a large and complex enzyme ; has multiple subunits and ~ 800 kD. Contains bound FAD, Mo, and cytochrome 557 and has ferredoxin Fe4S4 center. It is NADH/NADPH-dependent according to organism. Mo is bound to a cofactor containing a pteridine ring to form molybdopterin.
- Nitrite reductase (2, 3, 4) catalyzes the last three steps in the reduction of nitrate to NH3. Contains one ferredoxin Fe2S2 center and one molecule of siroheme (partially reduced Fe porphyrin) and the electron donor for each step is ferredoxin.
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Enzymes are proteins that catalyze (i.e. accelerate) chemical reactions.[1] In enzymatic reactions, the molecules at the beginning of the process are called substrates, and the enzyme converts them into different molecules, the products.
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Trinitrate redirects here. See also glyceryl trinitrate.
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nitrite ion is NO2−. The anion is bent, being isoelectronic with O3.
A nitrite is either a salt or an ester of nitrous acid.
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A nitrite is either a salt or an ester of nitrous acid.
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In biochemistry, flavin adenine dinucleotide (FAD) is the precursor molecule to FADH2. Upon bonding to two hydrogen atoms, FAD is then changed to FADH2 and is turned into an energy-carrying molecule.
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6
(strongly acidic oxide)
Electronegativity 2.16 (scale Pauling)
Ionization energies
(more) 1st: 684.3 kJmol−1
2nd: 1560 kJmol−1
3rd: 2618 kJmol−1
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(strongly acidic oxide)
Electronegativity 2.16 (scale Pauling)
Ionization energies
(more) 1st: 684.3 kJmol−1
2nd: 1560 kJmol−1
3rd: 2618 kJmol−1
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Cytochromes are generally membrane-bound hemoproteins that contain heme groups and carry out electron transport.
They are either found as monomeric proteins (i.e. cytochrome c) or as subunits of bigger enzymatic complexes that catalyze redox reactions.
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They are either found as monomeric proteins (i.e. cytochrome c) or as subunits of bigger enzymatic complexes that catalyze redox reactions.
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Ferredoxins (from Latin ferrum: iron + redox, often abbreviated "fd") are iron-sulfur proteins that mediate electron transfer in a range of metabolic reactions.
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Overview
The term "ferredoxin" was coined by D.C. Wharton of the DuPont Co...... Click the link for more information.
Cofactor may refer to any of the following:
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- Cofactor (linear algebra) The signed minor of a matrix
- Minor (linear algebra) as an alternative name for the determinant of a smaller matrix than that which it describes
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Pteridine is a chemical compound composed of fused pyrimidine and pyrazine rings. A pteridine is also a group of heterocyclic compounds containing a wide variety of substitutions on this structure.
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Molybdopterins are a class of biochemical cofactors that are used in many different enzymes. The simplest structure of molybdopterin contains a pyranopterin coordinated to molybdenum. The pyranopterin structure is a fused ring system containing a pyran fused to pterin.
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Ammonia is a compound with the formula NH3. It is normally encountered as a gas with a characteristic pungent odor. Ammonia contributes significantly to the nutritional needs of the planet as a precursor to foodstuffs and fertilizers.
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Ferredoxins (from Latin ferrum: iron + redox, often abbreviated "fd") are iron-sulfur proteins that mediate electron transfer in a range of metabolic reactions.
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Overview
The term "ferredoxin" was coined by D.C. Wharton of the DuPont Co...... Click the link for more information.
FE may refer to:
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- Fantasy Empires, a 1993 Dungeons & Dragons computer game
- Fast Ethernet
- Fe (album), The debut album by Souled American
- Fe (rune), the f-rune, ᚠ of the Younger Futhark
- Fe (Spanish language), the Spanish translation of the word 'faith'.
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porphyrin is a heterocyclic macrocycle derived from four pyrrole-like subunits interconnected via their α carbon atoms via methine bridges (=CH-). The macrocycle, therefore, is a highly conjugated system, and is consequently deeply coloured—the name porphyrin
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Electron
Theoretical estimates of the electron density for the first few hydrogen atom electron orbitals shown as cross-sections with color-coded probability density
Composition: Elementary particle
Family: Fermion
Group: Lepton
Generation: First
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Theoretical estimates of the electron density for the first few hydrogen atom electron orbitals shown as cross-sections with color-coded probability density
Composition: Elementary particle
Family: Fermion
Group: Lepton
Generation: First
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Orientations of Proteins in Membranes (OPM) database provides spatial positions of protein three-dimensional structures with respect to the lipid bilayer. [1] [2]. [2].
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Medical Subject Headings (MeSH) is a huge controlled vocabulary (or metadata system) for the purpose of indexing journal articles and books in the life sciences. Created and updated by the United States National Library of Medicine (NLM), it is used by the MEDLINE/PubMed
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Proteins are large organic compounds made of amino acids arranged in a linear chain and joined together by peptide bonds between the carboxyl and amino groups of adjacent amino acid residues.
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Flavoproteins are proteins that contain a nucleic acid derivative of riboflavin: the flavin adenine dinucleotide (FAD) or flavin mononucleotide (FMN).
Flavoproteins are involved in a wide array of biological processes, including, but by no means limited to, bioluminescence,
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Flavoproteins are involved in a wide array of biological processes, including, but by no means limited to, bioluminescence,
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The acetolactate synthase (ALS) enzyme (also known as acetohydroxyacid synthase, or AHAS) is the first step in the synthesis of the branched-chain amino acids (valine, leucine, and isoleucine).
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Acyl CoA dehydrogenase is the enzyme used to catalyze the first step of β-oxidation in Fatty acid metabolism.
The enzyme catalyzes the formation of a double bond between the C-2 and C-3.
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Reaction
The following reaction is the oxidation of the fatty acid by FAD.The enzyme catalyzes the formation of a double bond between the C-2 and C-3.
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Apoptosis inducing factor is a flavoprotein.
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See also
- Apoptosis
External links
- MeSH Apoptosis+inducing+factor
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Butyryl CoA dehydrogenase is a flavoprotein.
It acts upon butyryl-coenzyme A.
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It acts upon butyryl-coenzyme A.
See also
- Butyric_acid#Butyrate_fermentation
- Causes_of_hypoglycemia#Metabolic_Defects
External links
- MeSH Butyryl-CoA+Dehydrogenase
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Identifiers
Symbol CRY2
Entrez 1408
HUGO 2385
OMIM 603732
RefSeq NM_021117
UniProt Q49AN0
Other data
Locus Chr. 11 p11.2 Cryptochrome is a name used historically for the blue light photoreceptors of plants.
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Symbol CRY2
Entrez 1408
HUGO 2385
OMIM 603732
RefSeq NM_021117
UniProt Q49AN0
Other data
Locus Chr. 11 p11.2 Cryptochrome is a name used historically for the blue light photoreceptors of plants.
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Cytochrome-b5 reductase (CBR; EC 1.6.2.2 ) is a FAD-containing enzyme catalysing the reaction: NADH + H+ + 2 ferricytochrome b5 = NAD+ + 2 ferrocytochrome b5
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Dihydrolipoamide dehydrogenase is a flavoprotein enzyme which degrades lipoamide, and produces dihydrolipoamide.
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Lipoamide
Dihydrolipoamide
See also
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Flavodoxin is a bacterial protein that includes flavin mononucleotide. It contains five beta sheets.
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External links
- MeSH Flavodoxin
- "The crossovers of flavodoxin" at virginia.edu
- Diagram at tran.wau.nl
- Diagram at ohio-state.
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Methemoglobin reductase (also known as cytochrome-b5 reductase) is an enzyme which converts methemoglobin to hemoglobin.
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See also
- Methemoglobinemia
- Reductase
External links
- MeSH
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Methylenetetrahydrofolate reductase (MTHFR) is an enzyme (EC 1.5.1.20 ) that exists in the cytoplasm of cells. MTHFR contains a bound flavin cofactor and uses NAD(P)H as the reducing agent.
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NADH dehydrogenase (EC 1.6.5.3 ) is an enzyme located in the inner mitochodrial membrane that catalyzes the transfer of electrons from NADH to coenzyme Q (CoQ). It is also called the NADH:quinone oxidoreductase.
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