Article Evaluation
edit- Everything present is relevant to the article topic.
- There could be more added to the history section.
- There should be a subtopic created on "sulfate".
- The article itself is neutral and the viewpoints are underrepresented.
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-The references are reliable with the article and they all are neutral sources.
- Most of the information on this article are retrieved from peer-reviewed articles.
-There seems to be no bias topics on this article
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Week 3 Tasks - Info for 1,2-Diamino-5-bromo-3-chlorobenzene
editProperties of 1,2-Diamino-5-bromo-3-chlorobenzene
edit- Molecular formula: C6H6BrClN2
- Molar mass: 221.48 g/mol
- Melting point (m.p.): 57-60 oC
- Boiling point (b.p.): N/A
- Storage temperature: 2-8 oC
- Solubility in water: N/A
1,2-Diamino-5-bromo-3-chlorobenzene
1,2-Diamino-5-bromo-3-chlorobenzene [1]
References
edit"Dinitrogen Reduction: Interfacing the Enzyme Nitrogenase with Electrodes"[1] "Mechanistic insights into nitrogen fixation by nitrogenase enzymes" [2] "Energy Transduction in Nitrogenase" [3]
- ^ Fourmond, Vincent; Léger, Christophe (2017-03-16). "Dinitrogen Reduction: Interfacing the Enzyme Nitrogenase with Electrodes". Angewandte Chemie International Edition. 56 (16): 4388–4390. doi:10.1002/anie.201701179. ISSN 1433-7851.
- ^ Varley, J. B.; Wang, Y.; Chan, K.; Studt, F.; Nørskov, J. K. (2015). "Mechanistic insights into nitrogen fixation by nitrogenase enzymes". Physical Chemistry Chemical Physics. 17 (44): 29541–29547. doi:10.1039/c5cp04034e. ISSN 1463-9076.
- ^ Seefeldt, Lance C.; Hoffman, Brian M.; Peters, John W.; Raugei, Simone; Beratan, David N.; Antony, Edwin; Dean, Dennis R. (2018-08-10). "Energy Transduction in Nitrogenase". Accounts of Chemical Research. 51 (9): 2179–2186. doi:10.1021/acs.accounts.8b00112. ISSN 0001-4842.
| Functional groups | Bond type | Shift (ppm) | Splitting |
|---|---|---|---|
| Amine | NH2 | 4.82 | Doublet |
| Amine | NH2 | 4.94 | Doublet |
| sp2 - carbon | CH | 6.57 | Singlet |
| sp2 - carbon | CH | 7.03 | Singlet |
- Fraction:
- Exponent: 42
- Subscript: Td (tetrahedral)
|
| |
| Names | |
|---|---|
| IUPAC name
1,2-Diamino-5-bromo-3-chlorobenzene
| |
| Other names
5-Bromo-3-chlorobenzene-1,2-diamine
| |
| Identifiers | |
PubChem CID
|
|
| Properties | |
| C6H6BrClN2 | |
| Molar mass | 221.48 g/mol |
| Melting point | 57–60 °C (135–140 °F; 330–333 K) |
| Hazards | |
| Occupational safety and health (OHS/OSH): | |
Main hazards
|
Danger: skin corrosion/irritation |
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
| |
 | This is a user sandbox of Levarage16. You can use it for testing or practicing edits. This is not the sandbox where you should draft your assigned article for a dashboard.wikiedu.org course. To find the right sandbox for your assignment, visit your Dashboard course page and follow the Sandbox Draft link for your assigned article in the My Articles section. |
First 250 Words Assignment Topic
editI have chosen to write my first 250 words on "Urease" topic where I will discuss more on where urease is found in (mammal and humans) and also, what type of tissue and/or cells are included in the urea processing.
Urease
editUrease is also found in mammals and humans which is considered to be very harmful to the mammals due to production of the toxic ammonia product in the mammalian cells. However, mammalian cells does not produce urease in fact, the source is the various bacterias in the body, specifically the intestine. European hare (Lepus europaeus),a class of Mammalia, was discovered to have high urease activity in their large intestine, a part of gastrointestinal tract.[1] Previously, other mammals i.e. rats, pigs and rabbits, with postgastric fermentation were detected with lower urease activity compared to European Hare. [1] In human kidneys, urea is present in order for everyday functions and is estimated that per day, a healthy adult excretes about 10 to 30 g of urea.[2] Other than urea being found in urine, it is also present in sweat, blood serum and stomach.[2] Inside the liver cell (which is found to be in mitochondria), excess ammonia is converted to urea through the urea cycle and if some excess ammonia is still present in the mitochondria, then it gets used up for protein synthesis. There are specific tissues involved during urea processing which are epithelial, extrahepatic and muscle tissues.[3] With the production of ammonia and amino acids, the cell proteins are broken down by proteolytic enzymes already present in the muscle tissue.[4] Similarly, identical cell proteins are predicted to convert previously broken down ammonia into urea.[4] Once the urea is formed in the liver, it is excreted through urine after passing from bloodstream and the kidneys.
- ^ a b Stepan’kov, A. A.; Kuznetsova, T. A.; Vecherskii, M. V. (2017). "Urease activity in the gastrointestinal tract of the European hare (Lepus europaeus)". Biology Bulletin. 44 (2): 224–227. doi:10.1134/s1062359017020194. ISSN 1062-3590.
- ^ a b Konieczna, Iwona; Żarnowiec, Paulina; Kwinkowski, Marek; Kolesińska, Beata; Frączyk, Justyna; Kamiński, Zbigniew; Kaca, Wiesław (2012). "Bacterial Urease and its Role in Long-Lasting Human Diseases". Current Protein & Peptide Science. 13 (8): 789–806. doi:10.2174/138920312804871094. ISSN 1389-2037. PMC 3816311. PMID 23305365.
{{cite journal}}: CS1 maint: PMC format (link) - ^ 1942-, Nelson, David L. (David Lee), (2013). Lehninger principles of biochemistry. Cox, Michael M.,, Lehninger, Albert L. (6th ed ed.). New York: W.H. Freeman and Company. ISBN 9781429234146. OCLC 824794893.
{{cite book}}:|edition=has extra text (help);|last=has numeric name (help)CS1 maint: extra punctuation (link) CS1 maint: multiple names: authors list (link) - ^ a b "IS UREA FORMED IN THE MUSCLES?". Journal of the American Medical Association. LXIX (21): 1791. 1917-11-24. doi:10.1001/jama.1917.02590480045019. ISSN 0002-9955.
Second 25o words and 400 words contributions
editI have chosen "Urease" and "Nitrite Reductase" topics for my 250 & 400 words contributions.
- Describe and draw the Urease mechanism
- Needs a reaction equation for nitrite reductase
- Describe and draw the mechanism of nitrite reductase
Urease Mechanism
editThe mechanism starts off with the active site of Bacillus Pasteurii urease.[1] The first step of both cycle A and B involves the substitution of the more accessible water molecule with urea. Second step in cycle A involves the removal of the other water molecule. Followed by the attack on the organic carbonyl by the oxygen’s lone pair of the hydroxyl group. This result in the removal of a hydrogen ion, which will then be pick up by the amide (NH2). Oxygen then uses its lone pair to form a double bond in the complex and cleaves the ammonia group (NH3). Lastly, three water molecules rebuild the original state of the urease enzyme. Second step in cycle B involves the removal of a hydrogen ion from the other water molecule, making it a hydroxyl group. Then cycle B follows a similar mechanism to that seen in cycle A with the exception of the abstraction of hydrogen by the amide (NH2) group. At last, two water molecules restore the initial state of the urease enzyme.
- ^ Carlsson, Håkan; Nordlander, Ebbe (2010). "Computational Modeling of the Mechanism of Urease". Bioinorganic Chemistry and Applications. 2010: 1–8. doi:10.1155/2010/364891. ISSN 1565-3633. PMC 2945649. PMID 20886006.
{{cite journal}}: CS1 maint: PMC format (link) CS1 maint: unflagged free DOI (link)
Nitrite Reductase
editCopper containing nitrite reductase (NiR) catalyzes in reduction of one electron of nitrite to nitric oxide[2]:
NO2- + 2H+ + e- NO + H2O [2]
Latest schematic proposed mechanism: In cycle A, electron transfer from the copper (Cu) site takes place in the reaction which is followed by the proton transfer from the aspartate (Asp) catalytic residue.[3] Then, nitrogen oxide (NO) from the compound leaves the reaction. From Histidine catalytic residue, second proton transfer step occurs in order to form the resting nature.[3] As for cycle B, formation of nitrous acid (HONO) takes place by proton transfer from the aspartate (Asp) to nitrite. Second, the electron transfer step from copper (Cu) site is introduced.[3] At last, second proton enters in the reaction to form the resting state.[3]
- ^ Cite error: The named reference
:2was invoked but never defined (see the help page). - ^ a b Wijma, Hein J.; Jeuken, Lars J. C.; Verbeet, Martin Ph.; Armstrong, Fraser A.; Canters, Gerard W. (2007). "Protein Film Voltammetry of Copper-Containing Nitrite Reductase Reveals Reversible Inactivation". Journal of the American Chemical Society. 129 (27): 8557–8565. doi:10.1021/ja071274q. ISSN 0002-7863.
- ^ a b c d e Lintuluoto, Masami; Lintuluoto, Juha M. (2015-12-29). "DFT Study on Nitrite Reduction Mechanism in Copper-Containing Nitrite Reductase". Biochemistry. 55 (1): 210–223. doi:10.1021/acs.biochem.5b00542. ISSN 0006-2960.
- ^ Biological inorganic chemistry : structure and reactivity. Bertini, Ivano. Sausalito, Calif.: University Science Books. 2007. ISBN 1891389432. OCLC 65400780.
{{cite book}}: CS1 maint: others (link)