CooA

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CooA is a heme-containing transcription factor that responds to the presence of carbon monoxide. This protein forms homodimers and is a homolog of cAMP receptor protein. [1] CooA regulates the expression of carbon monoxide dehydrogenase, an enzyme that catalyzes the oxidation of CO to CO2. The most well-studied CooA homolog comes from Rhodospirillum rubrum (RrCooA), but the CooA homolog from Carboxydothermus hydrogenoformans (ChCooA) has been studied as well. [2] The main difference between these two CooA homologs is the ferric heme coordination. For RrCooA, the ferric heme iron is bound to a cysteine and the amine of the N-terminal proline, while, in the ferrous state, a ligand switch occurs where a nearby histidine displaces the thiolate. [3] [4] [5] For ChCooA, the heme iron is ligated by a histidine and the N-terminal amine in both the ferric and ferrous states. [6] For both homologs, CO displaces the amine ligand and activates the protein to bind to its target DNA sequence. [7] [8] Several structures of CooA exist: RrCooA in the ferrous state (1FT9), [9] ChCooA in the ferrous, imidazole-bound state (2FMY), [10] and ChCooA in the ferrous, CO-bound state (2HKX). [11]

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Histidine (symbol His or H) is an essential amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated –NH3+ form under biological conditions), a carboxylic acid group (which is in the deprotonated –COO form under biological conditions), and an imidazole side chain (which is partially protonated), classifying it as a positively charged amino acid at physiological pH. Initially thought essential only for infants, it has now been shown in longer-term studies to be essential for adults also. It is encoded by the codons CAU and CAC.

<span class="mw-page-title-main">Hemoprotein</span> Protein containing a heme prosthetic group

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<span class="mw-page-title-main">Heme</span> Chemical coordination complex of an iron ion chelated to a porphyrin

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<span class="mw-page-title-main">Metalloprotein</span> Protein that contains a metal ion cofactor

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Regulator of CO Metabolism (RcoM) is a heme-containing transcription factor found in bacteria that senses carbon monoxide (CO). In the presence of carbon monoxide, this protein upregulates expression of genes involved in carbon monoxide oxidation or carbon monoxide stress response. RcoM is functionally related to another heme-containing transcription factor, CooA, but RcoM shares no structural relationship with CooA. RcoM is composed of an N-terminal Per-Arnt-Sim (PAS) domain and a C-terminal LytTR domain. The PAS domain binds a single molecule of heme and the LytTR domain binds to DNA upstream of carbon monoxide oxidation genes. The RcoM homolog from Paraburkholderia xenovorans is known to be dimeric and binds heme using a histidine and a methionine ligand in the Fe(II) oxidation state. Carbon monoxide replaces the methionine ligand and binds directly to the heme to active RcoM for DNA binding. Relative to other heme-containing proteins, RcoM has an extraordinarily high CO affinity, with a Kd < 100 pM, allowing this protein to sense very low levels of carbon monoxide.

References

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