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Identification by ENDOR of Trp 191 as the Free-Radical Site in Cytochrome c Peroxidase Compound ES
Abstract
The chemical identity of the amino acid free-radical site that represents one of the two oxidizing equivalents stored in the H 2 O 2 -oxidized intermediate (compound ES) of the mitochondrial heme enzyme, cytochrome c peroxidase (CcP) has been sought for almost a quarter of a century. Site-directed mutagenesis alone cannot yield this answer. Low-temperature 35-gigahertz (Q-band) electron nuclear double resonance (ENDOR) spectroscopy was used to examine compound ES prepared from proteins containing specifically deuterated methionine or tryptophan, as well as the amino acid replacement Trp 51 → Phe. The results definitely identify the site of the radical in compound ES as tryptophan, most likely Trp 191 .
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Citations
Cited by
Heme Enzyme Structure and Function
Poulos, T. L. (2014) · Chemical Reviews · doi:10.1021/cr400415k · Cited by 1,443
Redox properties of heme peroxidases
Battistuzzi, G., Bellei, M., Bortolotti, C. A., & Sola, M. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.03.002 · Cited by 218
Poulos, T. L. (2007) · Natural Product Reports · doi:10.1039/b604195g · Cited by 69
Crystal structures of dye‐decolorizing peroxidase with ascorbic acid and 2,6‐dimethoxyphenol
Yoshida, T., Tsuge, H., Hisabori, T., & Sugano, Y. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.10.049 · Cited by 46
The diffusion-controlled reaction of semioxidized tryptophan with the superoxide radical anion
Santus, R., Patterson, L. K., & Bazin, M. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(95)00055-3 · Cited by 21
Santus, R., Patterson, L. K., Bazin, M., Mazière, J. C., & Morlière, P. (1998) · Free Radical Research · doi:10.1080/10715769800300451 · Cited by 9
Metadata
- Authors
- Sivaraja, M., Goodin, D. B., Smith, M., & Hoffman, B. M.
- Venue
- Science
- Published
- 1989-08-18
- Volume
- 245
- Issue
- 4919
- Pages
- 738-740
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2107277439
- Cited by
- 479
- References
- 0
- FWCI
- 22.16
- Type
- journal article
- Language
- en
- Open access
- closed
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