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Basis of guanylate cyclase activation by carbon monoxide.
Open accessAbstract
Kinetics of CO association with guanylate cyclase [GTP pyrophosphate-lyase (cyclizing), EC 4.6.1.2] and dissociation from carboxy guanylate cyclase have been studied at pH 7.5 by flash photolysis, yielding rate constants at 23 degrees C of 1.2 +/- 0.1 x 10(5) M-1.sec-1 and 28 +/- 2 sec-1, respectively. While the CO combination rate constant is the same as for the T state of hemoglobin, the CO dissociation rate constant is much higher than expected for a six-coordinate carboxyheme protein; yet the absorption spectrum is indicative of a six-coordinate heme. The two observations are reconciled by a reaction mechanism in which CO dissociation proceeds via a five-coordinate intermediate. This intermediate is structurally very similar to the five-coordinate nitrosyl heme derivative of guanylate cyclase and is presumably responsible for the observed 4-fold activation of guanylate cyclase by CO. Thus, we provide a model that explains enzyme activities of the nitrosyl and carboxy forms of the enzyme on the basis of a common mechanism.
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Cites
Stone, J. R., & Marletta, M. A. (1994) · Biochemistry · doi:10.1021/bi00184a036 · Cited by 647
Cited by
Riess, J. G. (2001) · Chemical Reviews · doi:10.1021/cr970143c · Cited by 773
Heme oxygenase/carbon monoxide signaling pathways: Regulation and functional significance
Ryter, S. W., Otterbein, L. E., Morse, D., & Choi, A. M. K. (2002) · Molecular and Cellular Biochemistry · doi:10.1023/a:1015957026924 · Cited by 497
A central role for free heme in the pathogenesis of severe malaria: the missing link?
Ferreira, A., Balla, J., Jeney, V., Balla, G., & Soares, M. P. (2008) · Journal of Molecular Medicine · doi:10.1007/s00109-008-0368-5 · Cited by 205
Cystathionine β-synthase and PGRMC1 as CO sensors
Kabe, Y., Yamamoto, T., Kajimura, M., Sugiura, Y., Koike, I., Ohmura, M., Nakamura, T., Tokumoto, Y., Tsugawa, H., Handa, H., et al. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.08.025 · Cited by 28
Metadata
- Authors
- Kharitonov, V. G., Sharma, V. S., Pilz, R. B., Magde, D., & Koesling, D.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1995-03-28
- Volume
- 92
- Issue
- 7
- Pages
- 2568-2571
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2051478582
- Cited by
- 207
- References
- 1
- FWCI
- 4.33
- Type
- journal article
- Language
- en
- Open access
- green
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- Kharitonov, V. G., Sharma, V. S., Pilz, R. B., Magde, D., & Koesling, D. (1995). Basis of guanylate cyclase activation by carbon monoxide. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.92.7.2568
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
