The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
The stereochemistry of peroxidase catalysis.
Open accessAbstract
A stereochemical mechanism is proposed for the per- oxidase-catalyzed heterolytic cleavage of the RO-OH bond. It is based on the 2.5 A structure of cytochrome c peroxidase, model building experiments, and an ex-tensive body of literature on peroxidase biochemistry. The essential features of this mechanism are acid-base catalysis by an invariant distal histidine (His-52 in cytochrome c peroxidase), charge stabilization by an invariant arginine residue (Arg-48), and stabilization of higher oxidation states of the heme iron atom by means of interaction between an invariant proximal histidine (His-174) and a nearby buried glutamine-glu-tamate pair (Gln-239, Glu-187). The indole ring of Trp-01 on the distal side of the heme ring is probably the site of radical formation in compound I of cytochrome c peroxidase. The essential role of the catalytic arginine in the proposed mechanism offers an explanation why peroxidase in
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Cites
LXXIII.—Oxidation of tartaric acid in presence of iron
Fenton, H. J. H. (1894) · J. Chem. Soc., Trans. · doi:10.1039/ct8946500899 · Cited by 3,179
Walling, C., & Goosen, A. (1973) · Journal of the American Chemical Society · doi:10.1021/ja00790a042 · Cited by 410
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Heme Enzyme Structure and Function
Poulos, T. L. (2014) · Chemical Reviews · doi:10.1021/cr400415k · Cited by 1,443
Self-citationCrystal structure of horseradish peroxidase C at 2.15 Å resolution
Gajhede, M., Schuller, D. J., Henriksen, A., Smith, A. T., & Poulos, T. L. (1997) · Nature Structural Biology · doi:10.1038/nsb1297-1032 · Cited by 710
Self-citationBelikova, N. A., Vladimirov, Y. A., Osipov, A. N., Kapralov, A. A., Tyurin, V. A., Potapovich, M. V., Basova, L. V., Peterson, J., Kurnikov, I. V., & Kagan, V. E. (2006) · Biochemistry · doi:10.1021/bi0525573 · Cited by 398
A Comprehensive Review on Function and Application of Plant Peroxidases
Pandey, V. P., Awasthi, M., Singh, S., Tiwari, S., & Dwivedi, U. N. (2017) · Biochemistry & Analytical Biochemistry · doi:10.4172/2161-1009.1000308 · Cited by 389
Active site structure and catalytic mechanisms of human peroxidases
Furtmüller, P. G., Zederbauer, M., Jantschko, W., Helm, J., Bogner, M., Jakopitsch, C., & Obinger, C. (2006) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2005.09.017 · Cited by 358
Metadata
- Authors
- Poulos, T. L., & Kraut, J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1980-09
- Volume
- 255
- Issue
- 17
- Pages
- 8199-8205
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1578742674
- Cited by
- 685
- References
- 2
- FWCI
- 16.66
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Poulos, T. L., & Kraut, J. (1980). The stereochemistry of peroxidase catalysis. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)70630-9
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