The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin
Open accessAbstract
The grail of protein science is the connection between structure and function. For myoglobin (Mb) this goal is close. Described as only a passive dioxygen storage protein in texts, we argue here that Mb is actually an allosteric enzyme that can catalyze reactions among small molecules. Studies of the structural, spectroscopic, and kinetic properties of Mb lead to a model that relates structure, energy landscape, dynamics, and function. Mb functions as a miniature chemical reactor, concentrating and orienting diatomic molecules such as NO, CO, O 2 , and H 2 O 2 in highly conserved internal cavities. Reactions can be controlled because Mb exists in distinct taxonomic substates with different catalytic properties and connectivities of internal cavities.
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Cites
Protein states and proteinquakes.
Ansari, A., Berendzen, J., Bowne, S. F., Frauenfelder, H., Iben, I. E., Sauke, T. B., Shyamsunder, E., & Young, R. D. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.15.5000 · Cited by 828
Self-citationOxidation of nitrogen-oxides by bound dioxygen in hemoproteins
Doyle, M. P., & Hoekstra, J. W. (1981) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(00)80291-3 · Cited by 643
Mechanism of NO-induced oxidation of myoglobin and hemoglobin
Eich, R. F., Li, T., Lemon, D. D., Doherty, D. H., Curry, S. R., Aitken, J. F., Mathews, A. J., Johnson, K. A., Smith, R. D., Phillips, et al. (1996) · Biochemistry · doi:10.1021/bi960442g · Cited by 613
Liu, X., Miller, M. J. S., Joshi, M. S., Thomas, D. D., & Lancaster, J. R. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.5.2175 · Cited by 602
Cited by
Berger, M. M., Shenkin, A., Schweinlin, A., Amrein, K., Augsburger, M., Biesalski, H.-K., Bischoff, S. C., Casaer, M. P., Gundogan, K., Lepp, H.-L., et al. (2022) · Clinical Nutrition · doi:10.1016/j.clnu.2022.02.015 · Cited by 615
Mechanistic aspects of the reactions of nitric oxide with transition-metal complexes
Ford, P. C., & Lorkovic, I. M. (2002) · Chemical Reviews · doi:10.1021/cr0000271 · Cited by 525
Fenimore, P. W., Frauenfelder, H., McMahon, B. H., & Young, R. D. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405573101 · Cited by 524
Self-citationWei, G., Xi, W., Nussinov, R., & Ma, B. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00562 · Cited by 436
Intrinsic dynamics of enzymes in the unbound state and relation to allosteric regulation
Bahar, I., Chennubhotla, C., & Tobi, D. (2007) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2007.09.011 · Cited by 306
Metadata
- Authors
- Frauenfelder, H., McMahon, B. H., Austin, R. H., Chu, K., & Groves, J. T.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2001-02-20
- Volume
- 98
- Issue
- 5
- Pages
- 2370-2374
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1968872901
- Cited by
- 340
- References
- 4
- FWCI
- 9.37
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Frauenfelder, H., McMahon, B. H., Austin, R. H., Chu, K., & Groves, J. T. (2001). The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.041614298
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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.
