The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Biochemical and spectroscopic characterization of catechol oxidase from sweet potatoes (Ipomoea batatas) containing a type‐3 dicopper center1
Abstract
Two catechol oxidases have been isolated from sweet potatoes (Ipomoea batatas) and purified to homogeneity. The two isozymes have been characterized by EXAFS, EPR‐, UV/Vis‐spectroscopy, isoelectric focusing, and MALDI‐MS and have been shown to contain a dinuclear copper center. Both are monomers with a molecular mass of 39 kDa and 40 kDa, respectively. Substrate specificity and NH 2‐terminal sequences have been determined. EXAFS data for the 39 kDa enzyme reveal a coordination number of four for each Cu in the resting form and suggest a Cu(II)‐Cu(II) distance of 2.9 Å for the native met form and 3.8 Å for the oxy form.
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Citations
Cites
Multicopper oxidases and oxygenases
Solomon, E. I., Sundaram, U. M., & Machonkin, T. E. (1996) · Chemical Reviews · doi:10.1021/cr950046o · Cited by 3,664
Matrix-assisted laser desorption/ionization mass spectrometry of biopolymers.
Hillenkamp, F., Karas, M., Beavis, R. C., & Chait, B. T. (1991) · Analytical Chemistry · doi:10.1021/ac00024a716 · Cited by 1,930
Cited by
Copper Active Sites in Biology
Solomon, E. I., Heppner, D. E., Johnston, E. M., Ginsbach, J. W., Cirera, J., Qayyum, M., Kieber-Emmons, M. T., Kjaergaard, C. H., Hadt, R. G., & Tian, L. (2014) · Chemical Reviews · doi:10.1021/cr400327t · Cited by 1,751
Crystal structure of a plant catechol oxidase containing a dicopper center
Klabunde, T., Eicken, C., Sacchettini, J. C., & Krebs, B. (1998) · Nature Structural Biology · doi:10.1038/4193 · Cited by 870
Self-citationThe Crystal Structure of Catechol Oxidase: New Insight into the Function of Type-3 Copper Proteins
Gerdemann, C., Eicken, C., & Krebs, B. (2002) · Accounts of Chemical Research · doi:10.1021/ar990019a · Cited by 585
Self-citationSynthetic models of the active site of catechol oxidase: mechanistic studies
Koval, I. A., Gamez, P., Belle, C., Selmeczi, K., & Reedijk, J. (2006) · Chemical Society Reviews · doi:10.1039/b516250p · Cited by 527
Tyrosinase/catecholoxidase activity of hemocyanins: structural basis and molecular mechanism
Decker, H., & Tuczek, F. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01602-9 · Cited by 377
Metadata
- Authors
- Eicken, C., Zippel, F., Büldt-Karentzopoulos, K., & Krebs, B.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1998-10-02
- Volume
- 436
- Issue
- 2
- Pages
- 293-299
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W1535193939
- Cited by
- 167
- References
- 2
- FWCI
- 4.38
- Type
- journal article
- Language
- en
- Open access
- closed
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- Eicken, C., Zippel, F., Büldt-Karentzopoulos, K., & Krebs, B. (1998). Biochemical and spectroscopic characterization of catechol oxidase from sweet potatoes (Ipomoea batatas) containing a type‐3 dicopper center1. FEBS Letters. https://doi.org/10.1016/s0014-5793(98)01113-2
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