The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Higher oxidation states of prostaglandin H synthase: EPR study of a transient tyrosyl radical in the enzyme during the peroxidase reaction
Open accessAbstract
Purified prostaglandin H synthase (EC 1.14.99.1), reconstituted with hemin, was reacted with substrates of the cyclooxygenase and peroxidase reaction. The resulting EPR spectra were measured below 90 K. Arachidonic acid, added under anaerobic conditions, did not change the EPR spectrum of the native enzyme due to high‐spin ferric heme. Arachidonic acid with O 2, as well as prostaglandin G 2 or H 2 O 2, decreased the spectrum of the native enzyme and concomitantly a doublet signal at g= 2.005 was formed with maximal intensity of 0.35 spins/enzyme and a half‐life of less than 20 s at ‐12 °C. From the conditions for the formation and the effect of inhibitors, this doublet signal was assigned to an enzyme intermediate of the peroxidase reaction, namely a higher oxidation state. The doublet signal with characteristic hyperfine structure was nearly identical to the signal of the tyrosyl radical in ribonucleotide reductase (EC 1.17.4.1). Hence the signal of prostaglandin H synthase was assigned to a tyrosyl radical. Electronic spectra as well as decreased power saturation of the tyrosyl radical signal indicated heme in its ferryl state which coupled to the tyrosyl radical weakly. [Fe IV O(protoporphyrin IX)]…Tyr+· was suggested as the structure of this two‐electron oxidized state of the enzyme. A hypothetical role for the tyrosyl radical could be the abstraction of a hydrogen at C‐13 of arachidonic acid which is assumed to be the initial step of the cyclooxygenase reaction.
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Cites
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Progress in the Chemistry of Organic Natural Products 109
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Cited by
Cyclooxygenases: Structural, cellular, and molecular biology
Smith, W. L., DeWitt, D. L., & Garavito, R. M. (2000) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.69.1.145 · Cited by 2,925
Protein Radicals in Enzyme Catalysis
Stubbe, J., & van der Donk, W. A. (1998) · Chemical Reviews · doi:10.1021/cr9400875 · Cited by 1,377
Three-dimensional structure of the free radical protein of ribonucleotide reductase
Nordlund, P., Sjöberg, B.-M., & Eklund, H. (1990) · Nature · doi:10.1038/345593a0 · Cited by 835
Imai, H., & Nakagawa, Y. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01197-8 · Cited by 767
Davis, K. L., Martin, E., Turko, I. V., & Murad, F. (2001) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.41.1.203 · Cited by 584
Metadata
- Authors
- KARTHEIN, R., DIETZ, R., NASTAINCZYK, W., & RUF, H. H.
- Venue
- European Journal of Biochemistry
- Publisher
- Wiley
- Published
- 1988-01
- Volume
- 171
- Issue
- 1-2
- Pages
- 313-320
- ISSN
- 0014-2956 (ISSN-L)
- 1432-1033
- OpenAlex
- W2894728782
- Cited by
- 284
- References
- 31
- FWCI
- 16.03
- Type
- journal article
- Language
- en
- Open access
- bronze
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- KARTHEIN, R., DIETZ, R., NASTAINCZYK, W., & RUF, H. H. (1988). Higher oxidation states of prostaglandin H synthase: EPR study of a transient tyrosyl radical in the enzyme during the peroxidase reaction. European Journal of Biochemistry. https://doi.org/10.1111/j.1432-1033.1988.tb13792.x
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