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]
^H. Körner; H. J. Sofia; W. G. Zumft (2003). "Phylogeny of the bacterial superfamily of Crp-Fnr transcription regulators: exploiting the metabolic spectrum by controlling alternative gene programs". FEMS Microbiology Reviews. 27 (5): 559–592. doi:10.1016/S0168-6445(03)00066-4. PMID 14638413.
^T. Shimizu; D. Huang; F. Yan; M. Stranava; M. Bartosova; V. Fojtíková; M. Martínková (2015). "Gaseous O2, NO, and CO in Signal Transduction: Structure and Function Relationships of Heme-Based Gas Sensors and Heme-Redox Sensors". Chem. Rev. 115 (13): 6491–6533. doi:10.1021/acs.chemrev.5b00018. PMID 26021768.
^Shelver, Daniel; Thorsteinsson, Marc V.; Kerby, Robert L.; Chung, Soo-Yeol; Roberts, Gary P.; Reynolds, Mark F.; Parks, Ryan B.; Burstyn, Judith N. (1999-03-01). "Identification of Two Important Heme Site Residues (Cysteine 75 and Histidine 77) in CooA, the CO-Sensing Transcription Factor of Rhodospirillum rubrum". Biochemistry. 38 (9): 2669–2678. doi:10.1021/bi982658j. ISSN 0006-2960. PMID 10052937.
^Dhawan, Ish K.; Shelver, Daniel; Thorsteinsson, Marc V.; Roberts, Gary P.; Johnson, Michael K. (1999-09-01). "Probing the Heme Axial Ligation in the CO-Sensing CooA Protein with Magnetic Circular Dichroism Spectroscopy". Biochemistry. 38 (39): 12805–12813. doi:10.1021/bi991303c. ISSN 0006-2960. PMID 10504250.
^Clark, Robert W.; Youn, Hwan; Parks, Ryan B.; Cherney, Melisa M.; Roberts, Gary P.; Burstyn, Judith N. (2004-11-01). "Investigation of the Role of the N-Terminal Proline, the Distal Heme Ligand in the CO Sensor CooA". Biochemistry. 43 (44): 14149–14160. doi:10.1021/bi0487948. ISSN 0006-2960. PMID 15518565.
^Inagaki, Sayaka; Masuda, Chiaki; Akaishi, Tetsuhiro; Nakajima, Hiroshi; Yoshioka, Shiro; Ohta, Takehiro; Pal, Biswajit; Kitagawa, Teizo; Aono, Shigetoshi (February 2005). "Spectroscopic and Redox Properties of a CooA Homologue from Carboxydothermus hydrogenoformans". Journal of Biological Chemistry. 280 (5): 3269–3274. doi:10.1074/jbc.m409884200. ISSN 0021-9258. PMID 15537640.
^G. P. Roberts; R. L. Kerby; H. Youn; M. Conrad (2005). "CooA, A Paradigm for Gas Sensing Regulatory Proteins". J. Inorg. Biochem. 99 (1): 280–92. doi:10.1016/j.jinorgbio.2004.10.032. PMID 15598507.
^Shigetoshi Aono (2003). "Biochemical and Biophysical Properties of the CO-Sensing Transcriptional Activator CooA". Acc. Chem. Res. 36 (11): 825–31. doi:10.1021/ar020097p. PMID 14622029.
^Lanzilotta, William N.; Schuller, David J.; Thorsteinsson, Marc V.; Kerby, Robert L.; Roberts, Gary P.; Poulos, Thomas L. (October 2000). "Structure of the CO sensing transcription activator CooA". Nature Structural Biology. 7 (10): 876–880. doi:10.1038/82820. ISSN 1545-9985. PMID 11017196. S2CID 26285016.
^Borjigin, M.; Li, H.; Lanz, N. D.; Kerby, R. L.; Roberts, G. P.; Poulos, T. L. (2007-03-01). "Structure-based hypothesis on the activation of the CO-sensing transcription factor CooA". Acta Crystallographica Section D: Biological Crystallography. 63 (3): 282–287. Bibcode:2007AcCrD..63..282B. doi:10.1107/S0907444906051638. ISSN 0907-4449. PMID 17327664.
(RrCooA), but the CooA homolog from Carboxydothermus hydrogenoformans (ChCooA) has been studied as well. The main difference between these two CooA homologs...
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