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Chloroperoxidase
Open accessAbstract
Chloroperoxidase from Caldariomyces fumago has been isolated in crystalline form. The prosthetic group of chloroperoxidase is ferriprotoporphyrin IX. On the basis of the heme content, the minimal molecular weight of chloroperoxidase is 40,200. On the basis of hydrodynamic measurements, the molecular weight of chloroperoxidase is approximately 42,000. Therefore, in solution at neutral pH, chloroperoxidase behaves as a monomeric species. The spectral properties of the oxidized and reduced forms of the enzyme and also of the azide and cyanide complexes are reported. The amino acid composition of chloroperoxidase is reported. Chloroperoxidase is rich in aspartic acid, glutamic acid, and serine and proline residues. These four amino acids constitute 45% of the total amino acid content. Chloroperoxidase is a glycoprotein. Approximately 25 to 30% of the molecule is carbohydrate. Chromatography of acid hydrolysates reveals that glucosamine and arabinose are major constituents.
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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
New and classic families of secreted fungal heme peroxidases
Hofrichter, M., Ullrich, R., Pecyna, M. J., Liers, C., & Lundell, T. (2010) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-010-2633-0 · Cited by 527
Ullrich, R., Nüske, J., Scheibner, K., Spantzel, J., & Hofrichter, M. (2004) · Applied and Environmental Microbiology · doi:10.1128/aem.70.8.4575-4581.2004 · Cited by 366
Comparison of ligninase-I and peroxidase-M2 from the white-rot fungus Phanerochaete chrysosporium
Paszczyński, A., Huynh, V.-B., & Crawford, R. (1986) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(86)90644-2 · Cited by 360
Synthetic Fe/Cu Complexes: Toward Understanding Heme-Copper Oxidase Structure and Function
Adam, S. M., Wijeratne, G. B., Rogler, P. J., Diaz, D. E., Quist, D. A., Liu, J. J., & Karlin, K. D. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00074 · Cited by 264
Metadata
- Authors
- Morris, D. R., & Hager, L. P.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1966-04
- Volume
- 241
- Issue
- 8
- Pages
- 1763-1768
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1567978295
- Cited by
- 534
- References
- 0
- FWCI
- 9.07
- Type
- journal article
- Language
- en
- Open access
- hybrid
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