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Week 3 Tasks - Info for Chromium(III) Acetate^{SuperscriptExample}_{SubScriptExample}

Chromium (iii) Acetate

Names
IUPAC name Chromium (iii) Acetate Hydrate
Identifiers
CAS Number	N/A
PubChem CID	14012
Properties
Chemical formula	C6H9O6Cr
Molar mass	229.1g/mol
Appearance	Blue Crystals
Melting point	N/A
Boiling point	N/A
Solubility in water	675g/L (20C, pH 5)
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).

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  Example picture. (Example external link)

Aromaticity (Example internal link)

Example math formulas

${\frac {9}{32}}$

$3^{3}=27$

$5345x_{3}+12x_{2}+65x$

Properties of Chromium(III) Acetate

• Molecular formula - C₆H₉O₆Cr
• Molar mass - 229.1 g/mol
• Melting point - N/A
• Boiling point - N/A
• Solubility (In water: 20^oC, pH 5) - 675 g/L

Chromium(III) Acetate

IR Spectrum Data

IR Peaks (nm)	Chemical Properties
2900	Molar mass: 229.1 g/mol
1450	Solubility: 675g/L
650

Article Examples

"Interspecies Homology of Nitrogenase genes"

"Isolation of an Iron-molybdenum cofactor from Nitrogenase"

"Evidence for Interstitial Carbon in Nitrogenase FeMo cofactor"

Carbon Monoxide Dehydrogenase (Early Contribution Revision+400 Word Equivalent)

The chemical process catalyzed by Carbon Monoxide Dehydrogenase is referred to as a water-gas shift reaction.

CO₂ reduction requires quick and efficient electron transfers to deliver necessary electrons to a redox catalyst. Therefore, a variety of electron donors/receivers (Shown as "A" and "AH₂" in the reaction equation above) are observed in micro-organisms which utilize CODH. Several examples of electron transfer cofactors include Ferredoxin, NADP+/NADPH and flavoprotein complexes like flavin adenine dinucleotide (FAD).

Microbial organisms (Both Aerobic and Anaerobic) encode and synthesize CODH for the purpose of carbon fixation (CO oxidation and CO₂ reduction). Depending on attached accessory proteins (A,B,C,D-Clusters), serve a variety of catalytic functions, including reduction of [4Fe-4S] clusters and insertion of Nickel.

Classes (Adding onto the wiki article's section)

Based on the microbe's environmental conditions, different metal complex centers are synthesized. Aerobic carboxydotrophic bacteria utilize Copper (Cu),Molybdenum (Mo) and Iron (Fe) based flavoenzymes. Anaerobic bacteria utilize Nickel (Ni) and Iron (Fe) based CODHs due to their oxygen sensitive nature.

Structure (Adding onto the wiki article's section)

Homodimeric Ni-CODH consists of five metal complexes referred to as clusters. ..., each differing in individual coordination geometry, presence of Nickel, and location of the active site in either sub-unit α or β.

Industrial Use (New Wiki Article Subheading)

Carbon monoxide dehydrogenase's or bio-mimetic complexes based on its catalytic potential in the formation of CO from CO_2, shows potential future catalytic uses in industrial processes. Potential candidates include the production of CH₃OH (Acetic acid) from CO in processes found in the Cativa process and Monsanto process. Production of CO as a precursor for liquid hydrocarbons, in the Fischer-Trophsch process.

Environmental relevance (Adding onto the wiki article's section)

Carbon Monoxide dehydrogenase is closely associated with the regulation of atmospheric CO and CO₂ levels, maintaining optimal CO levels suitable for other forms of life. Microbial organisms rely on these enzymes for both energy conservation along with CO₂ fixation. Often encoding for and synthesizing multiple unique forms of CODH for designated use. Further research into specific types of CODH show CO being used and condensed with CH₃ (Methyl groups) to form Acetyl-CoA. Anaerobic micro-organisms like Acetogens undergo the Wood-Ljungdahl Pathway, relying on CODH to produce CO by reduction of CO₂ needed for the synthesis of Acetyl-CoA from a methyl,coenzyme a (CoA) and corrinoid iron-sulfur protein. Other types show CODH being utilized to generate a proton motive force for the purposes of energy generation. CODH is used for the CO oxidation, producing two protons which are subsequently reduced to form dihydrogen (H₂, known colloquially as molecular hydrogen), providing the necessary free energy to drive ATP generation.

Structural diagram for Bifunctional CODH/ACS (A-Cluster). R = Ligand

Structural diagram for Bifunctional CODH/ACS (C-Cluster). R = Ligand

Structural diagram for Bifunctional CODH/ACS (D-Cluster)

Structural diagram for Bifunctional CODH/ACS (B-Cluster)