User:BillNye08

Molecular Formula: Cl₄Zn^-2[1]

Molar Mass: 207.2 g/mol

Melting Point: N/A

Boiling Point: N/A

Solubility in H₂O: N/A

1.3) Tetrachlorozincate^[2]

Mixed metal double salt ionic liquids comprised of [HN₂₂₂]₂[ZnCl₄] and AlCl₃ provide tunable Lewis acid catalysts related to the ionic environment^[3]

Aggregation of acridine orange: Crystal structure of acridine orange tetrachlorozincate 2C17H19N3·2HCl·ZnCl2·CH3COOH^[4]

Synthesis, Characterization, and Investigation of the Antimicrobial Activity of Cetylpyridinium Tetrachlorozincate^[5]

The figure provided by Bilal.bhatti96 does not include enough of a description on what the mechanism is showing, there should have been a a clear starting point to the mechanism . The arrows in the mechanism are not centered correctly, and there are some bonds that are not of equal length as would be expected in this proper mechanism. The figure is poorly organized as it is hard to determine what are starting materials and what are products.

${\displaystyle a_{c}=\left({\frac {v^{2}}{r}}\right)}$

The two edits made by Smokefoot were regarding the amount of unnecessary words as they implied that this article sounded more like an essay rather than a scientific article presenting facts. The comments that Smokefoot left in the talk page show that the article definitely needed some more editing before being published. The paragraphs that Ninja Rec contributed to this article were significantly shortened by Smokefoot which is why there is negative numbers in front of their contributions. This means that Smokefoot removed that specific amount of characters from the previous edit made by Ninja Rec. These two edits were necessary to beneficially contribute to a better scientific version of the article presented as they removed the parts that were not needed.

Hello,

I hoping to contribute, my knowledge to this article by discussing the strength, covalency and electron transfer effects. Ninja Recs (talk) 01:00, 12 October 2018 (UTC)

You are writing at a level that indicates that your teacher is needed. Please ask your teacher to read some Wikipedia articles first. --Smokefoot (talk) 01:20, 5 December 2018 (UTC)

Ninja Recs's Instructor gave 58 revisions to make to this contribution before moving to the live article however, regrettably, none of them were made --Kcsunshine999 (talk) 22:46, 5 September 2021 (UTC)

The three edits made4 by Smokefoot do the same thing as the previous article as they mention that there is some redundancy with the new material the Bilal.bhatti96 contributed. This is most likely due to not reading the pre-existing article before making new additions. Smokefoot made changes to the way that the sentences were formed as well as removing a bulk amount of redundant material from the article. The reason that there are negative numbers associated with the edits made by Smokefoot is because they removed that amount of characters to create a smoother flowing article.

I feel that this edit certainly makes an improvement to the introduction of this article because it gets rid of all the unnecessary material about the discovery of the enzyme, as well as it cleans up some of the run-off sentences. One thing that I would have changed to the Smokefoot edit would be that the stand alone sentence about how the enzyme maintains acid-base equilibrium does not make sense as it is written here. As corrected later on in the editing history, the sentence need little grammar corrections to flow on a more academic level.

The contribution made by Bilal.bhatti96 on November 28th 2019 was a great addition to the article and this is supported based on the fact that it remained on the Wikipedia article for a long time without being modified. Even on the current version of this article, the paragraph added on the Bohr effect is still included and therefore, it is a good addition to this article. The previous edit did not include any information on the Bohr effect and that means that the added information contributes to the overall point of the article.

This article has more discussion occuring in the talk page than the previous article investigated in this assignment, but in all cases, the more discussion the better. So it is hard to say whether or not there is enough useful discussion on what to improve with this article. That being said, some of the discussion posts more recently seem to miss the overall point of the article and also seem to dwell on less important facts such as why soda goes flat.

Topics - making a better introduction as well as editing the previous material

Peptidyl-Dipeptidase Dcp is a metalloprotein found in in the cytoplasm of bacterium E. Coli responsible for the C-terminal cleavage of a variety of dipeptides and unprotected larger peptide chains^[8]. The enzyme is comprised of 680 amino acid residues which organize into monomers to aid in the intracellular degradation of peptides^[9]. Metallic divalent cations inhibit the function of the enzyme Dcp which coordinated to divalent zinc which sits in the pocket of the active site, and is composed of four subsites: S₁’, S₁, S₂, and S₃^[10] .Basic amino acids accumulate at the S₁ site, The S₂ site sits deeper into the enzyme and has limited access to hydrophobic amino acids. Since amino acids prefer to be located at certain regions of the enzyme, it enhances the selectivity and proves the enzyme has high specificity for certain properties of amino acids. A pair of histidine residues bind to the catalytic zinc ion in similar fashion as reported by Menach et al^[11].  The enzyme is vertically elongated and has a deeper inner cavity where the active site is and is divided into two subdomains (I, and II).^[8] Peptidyl-Dipeptidase Dcp is classified like oligopeptidase A and Angiotensin-I converting enzyme (ACE) due to structural comparability but must be examined separately based on their discrepancy of peptidase activity. ACE has endopeptidase activity, whereas Dcp strictly has exopeptidase activity based on its cytoplasmic location and therefore their mechanisms of action are differentiated. Another difference between these enzymes is that the activity of Peptidyl-Dipeptidase Dcp is not enhanced in the presence of chloride anions, which is not the case for ACE.^[12]

Dcp is comprised of 680 amino acid residues that form into a single active monomer which aids in the intracellular degradation of peptides. Dcp coordinates to divalent zinc which sits in the pocket of the active site and is composed of four subsites : S₁’, S₁, S₂, and S₃, each subsite attracts certain amino acids at a specific position on the substrate enhancing the selectivity of the enzyme. The four subsites detect and bind different amino acid types on the substrate peptide in the P1 and P2 positions. Some metallic divalent cations such as Ni⁺², Cu⁺², and Zn⁺² inhibit the function of the enzyme around 90%, whereas other cations such as Mn⁺², Ca⁺², Mg⁺², and Co⁺² have slight catalyzing properties, and increase the function by around 20%. Basic amino acids such as Arginine bind preferably at the S₁ site, the S₂ site sits deeper in the enzyme therefore is restricted to bind hydrophobic amino acids  with phenylalanine in the P2 position. Dcp is divided into two subdomains (I, and II), which are the two sides of the clam shell-like structure and has a deep inner cavity where a pair of histidine residues bind to the catalytic zinc ion in the active site. Peptidyl-Dipeptidase Dcp is classified like Angiotensin-I converting enzyme (ACE) which is also a carboxypeptidase involved in blood pressure regulation, but due to structural differences and peptidase activity between these two enzymes, they had to be examined separately. ACE has endopeptidase activity, whereas Dcp strictly has exopeptidase activity based on its cytoplasmic location and therefore their mechanisms of action are differentiated. Another difference between these enzymes is that the activity of Peptidyl-Dipeptidase Dcp is not enhanced in the presence of chloride anions, whereas chloride enhances ACE activity.

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