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Week3 Tasks - Info for Cobalt(II) cyanide

Properties of Cobalt(II) cyanide

• Molecular formula: CO(CN)₂
• Molecular Weight: 110.97 g/mol
• Melting point: N/A
• Boiling point: N/A
• Solubility in water: N/A

Cobalt(II) cyanide

Cobalt(II) cyanide

Cobalt

Pubchem Properties for Cobalt(II) cyanide

Nitrogenase activity by diazotrophs grown on a range of agricultural plant residues.

Evidence for the occurrence of an alternative nitrogenase system in Azospirillum brasilense

Studies on the Relation Between Net Photosynthesis and Nitrogenase-linked Respiration in Subterranean Clover

Practice Uploading a PDB Structure Image

Critique of Carbonic Anhydrase Mechanism Figure

In the second compound, the double bonded oxygen has its bonds off-center. This issue occurs again on the 4th compound.

Bond angles are incorrect for the carbon dioxide of the first step, as well as for the carboxylic acid groups throughout the reaction.

The arrow brining water into the second step is inappropriately drawn (wrong bending angle).

The arrowheads to indicate reaction direction are too big.

Practice Making a Table

Property	Data
Molecular Formula	CO(CN)2
Molecular Weight	110.97 g/mol

Practice Entering a Formula

$X_{1}={1 \over 2}+e^{1}-y$

Practice Making a Chemical Information Box

Cobalt(II) cyanide

Names
IUPAC names cobalt(2+);dicyanide
Properties
Chemical formula	Co(CN)2
Molar mass	110.97 g/mol
Melting point	N/A
Boiling point	N/A
Solubility in water	N/A
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).

Practice Using History Pages, Talk pages, Article ratings and Watchlists

The main reason that the two edits were made by Smokefoot is to remove and replace the portions of text that portrays an essay instead of a collection of facts.

The statistics for these edits are negative numbers because they represent the net change in the bytes of text during the edit. In this case, a massive portion of text was removed, leading to the negative number.

I believe these edits were necessary as the previous structure of the information was formatted as an essay or an article that also contained grammatical errors. The previous structure attempted to analyze information from experiments rather than presenting the data.

Wikipedia “Iron–sulfur cluster” article: Talk page discussion of Dec 4th / 5th 2018 edits

Proposal

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)

In the Carbonic anhydrase article, Smokefoot made the three edits for the purpose of removing redundancy, adding a portion explaining the mechanism, and removing a repeated citation.

The negative statistics in the history page for these three edits indicate the removal of certain amounts of information represented in bytes.

The first edit made by Smokefoot was not an improvement as it removes details from the original text, as well as introducing more grammatical issues. However, the original text was formatted in an opinionated way (the enzyme's most important function), so it still needs improvement.

The Nov 28 2019 edit by Bilal was an improvement. However, explaining the Bohr effect in this paragraph was unnecessary since an internal link would have sufficed. This would allow more of a focus on the Carbonic anhydrase topic rather than explaining what the Bohr effect is.

The current version of the Carbonic anhydrase article still has the paragraph added by Bilal.

I believe the Talk tab of the Carbonic anhydrase article has a decent amount of useful discussion to improve the article, as there are people challenging the content, while the authors defend it with their citations. The discussions did seem to get quite heated though.

C This article has been rated as Low-importance on the project's importance scale.

Low This article has been rated as Low-importance on the project's importance scale.

First 250 Words

Subtopics:

• Entatic state: Update contribution in regards to instructor feedback on previous submission.
  • Explain the Entatic state principle and how it is thought to apply to the Blue Copper Proteins
  • Discuss unusually long Cu-S(Met) and short Cu-S(cys) bonds and the distorted “flattened” tetrahedral geometry

Types of Contributions:

• Adding new content for Entatic state
• Add citations for subtopics discussed

First 250 Words: Entatic State

Four-coordinate copper complexes often exhibit square planar geometry, however unique cases such as plastocyanin displays a distorted tetrahedral geometry. This unusual geometry is due to the entatic state of the protein. Plastocyanin performs electron transfer with the redox between Cu(I) and Cu(II), and it was first theorized that its entatic state was a result of the protein imposing the geometry of Cu(I) onto the oxidized Cu(II) site. However, recent studies have shown that this is not the case. Instead, the entatic state is defined as a protein environment that is capable of preventing ligand dissociation due to entropy increase from high temperatures. In the case of plastocyanin, the presence of a long and weak Cu(I)-S_Met bond at physiological temperatures does not dissociate due to the constraints of the protein environment, resulting in an entatic state.

The entatic state typically corresponds to the presence of a Jahn-Teller distorting force on the oxidized site. However, the Jahn-Teller distorting force is not present in plastocyanin due to a large split of the d_x2-y2 and d_xy­ orbitals. Additionally, the structure of plastocyanin exhibits a long Cu(I)-S_Met bond (2.8Å) with decreased electron donation strength. This bond also shortens the Cu(I)-S_Cys bond (2.1Å), increasing its electron donating strength. Overall, plastocyanin exhibits a lower reorganizational energy due to the entatic state, enabling it to perform electron transfer at a faster rate.

The properties associated with the entatic state of plastocyanin is also seen in other blue copper proteins, also known as Type I copper proteins. Other blue copper proteins possess similar ligand characteristics as plastocyanin but exhibit unique spectral properties. Such is the case of nitrite reductase, which has a green copper site.

First 250 Words Revision + 250 Word Equiv. Figure

Copper site of Plastocyanin from PDB 1AG6 showing the distorted tetrahedral geometry with the elongated Cu(I)-S_Met and shortened Cu(I)-S_Cys bonds.

Four-coordinate copper complexes often exhibit square planar geometry, however plastocyanin has a trigonally distorted tetrahedral geometry. This distorted geometry is less stable than ideal tetrahedral geometry due to its lower ligand field stabilization as a result of the trigonal distortion. This unusual geometry is induced by the rigid “pre-organized” conformation of the ligand donors by the protein, which is an entatic state. Plastocyanin performs electron transfer with the redox between Cu(I) and Cu(II), and it was first theorized that its entatic state was a result of the protein imposing an undistorted tetrahedral geometry preferred by ordinary Cu(I) complexes onto the oxidized Cu(II) site. However, a highly distorted tetrahedral geometry is induced upon the oxidized Cu(II) site instead of a perfectly symmetric tetrahedral geometry. A feature of the entatic state is a protein environment that is capable of preventing ligand dissociation even at a high enough temperature to break the metal-ligand bond. In the case of plastocyanin, it has been experimentally determined through absorption spectroscopy that there is a long and weak Cu(I)-S_Met bond that should dissociate at physiological temperature due to increased entropy. However, this bond does not dissociate due to the constraints of the protein environment dominating over the entropic forces.

Copper site of Plastocyanin showing the large splitting of the Cu d_x2-y2 and S_Cys d_xy­ orbitals.

In ordinary copper complexes involved in Cu(I)/Cu(II) redox coupling without a constraining protein environment, their ligand geometry changes significantly, and typically corresponds to the presence of a Jahn-Teller distorting force. However, the Jahn-Teller distorting force is not present in plastocyanin due to a large splitting of the d_x2-y2 and d_xy­ orbitals (See Blue Copper Protein Entatic State). Additionally, the structure of plastocyanin exhibits a long Cu(I)-S_Met bond (2.9Å) with decreased electron donation strength. This bond also shortens the Cu(I)-S_Cys bond (2.1Å), increasing its electron donating strength. Overall, plastocyanin exhibits a lower reorganization energy due to the entatic state of the protein ligand enforcing the same distorted tetrahedral geometry in both the Cu(II) and Cu(I) oxidations states, enabling it to perform electron transfer at a faster rate. The reorganization energy of blue copper proteins such as plastocyanin from 0.7 – 1.2 eV compared to 2.4 eV in an ordinary copper complex such as [Cu(phen)₂]^2+/+.