The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
A kinetic study on the suicide inactivation of peroxidase by hydrogen peroxide
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Citations
Cites
Childs, R. E., & Bardsley, W. G. (1975) · Biochemical Journal · doi:10.1042/bj1450093 · Cited by 893
Keilin, D., & Hartree, E. F. (1951) · Biochemical Journal · doi:10.1042/bj0490088 · Cited by 577
Mechanism of the disproportionation of superoxide radicals
Bielski, B. H. J., & Allen, A. O. (1977) · The Journal of Physical Chemistry · doi:10.1021/j100526a005 · Cited by 478
Chance, B. (1952) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(52)90470-0 · Cited by 280
Hayashi, Y., & Yamazaki, I. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86816-3 · Cited by 245
The Reaction of Ferrous Horseradish Peroxidase with Hydrogen Peroxide
Noble, R. W., & Gibson, Q. H. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63167-9 · Cited by 190
Inactivation of peroxidase by hydrogen peroxide and its protection by a reductant agent
Arnao, M. B., Acosta, M., del Rio, J. A., & García-Cánovas, F. (1990) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(90)90014-7 · Cited by 178
Self-citationThe mechanism of oxyperoxidase formation from ferryl peroxidase and hydrogen peroxide.
Nakajima, R., & Yamazaki, I. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61544-3 · Cited by 167
The mechanism of indole-3-acetic acid oxidation by horseradish peroxidases.
Nakajima, R., & Yamazaki, I. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37885-7 · Cited by 95
Cited by
Enzyme-mediated fast in situ formation of hydrogels from dextran–tyramine conjugates
Jin, R., Hiemstra, C., Zhong, Z., & Feijen, J. (2007) · Biomaterials · doi:10.1016/j.biomaterials.2007.02.032 · Cited by 422
Enzymology and structure of catalases
Nicholls, P., Fita, I., & Loewen, P. C. (2000) · Advances in Inorganic Chemistry · doi:10.1016/s0898-8838(00)51001-0 · Cited by 311
Asati, A., Kaittanis, C., Santra, S., & Perez, J. M. (2011) · Analytical Chemistry · doi:10.1021/ac102826k · Cited by 269
Serrano-Martínez, A., Fortea, M. I., del Amor, F. M., & Núñez-Delicado, E. (2008) · Food Chemistry · doi:10.1016/j.foodchem.2007.08.028 · Cited by 61
Metadata
- Authors
- Arnao, M. B., Acosta, M., del Rio, J. A., Varón, R., & García-Cánovas, F.
- Venue
- Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Publisher
- Elsevier BV
- Published
- 1990-10
- Volume
- 1041
- Issue
- 1
- Pages
- 43-47
- ISSN
- 0167-4838 (ISSN-L)
- OpenAlex
- W2001209511
- Cited by
- 281
- References
- 9
- FWCI
- 4.55
- Type
- journal article
- Language
- en
- Open access
- closed
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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- This page
- CoChat. (2026). Citation check: A kinetic study on the suicide inactivation of peroxidase by hydrogen peroxide. https://app.cochat.ai/papers/10.1016/0167-4838(90)90120-5
- The paper
- Arnao, M. B., Acosta, M., del Rio, J. A., Varón, R., & García-Cánovas, F. (1990). A kinetic study on the suicide inactivation of peroxidase by hydrogen peroxide. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. https://doi.org/10.1016/0167-4838(90)90120-5
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.