A novel resting form of the trinuclear copper center in the double mutant of a multicopper oxidase, CueO, Cys500Ser/Glu506Ala
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Abstract
A multicopper oxidase, CueO was doubly mutated at its type I copper ligand, Cys500 and an acidic amino acid residue located in the proton transfer pathway, Glu506, to Ser and Ala, respectively. Cys500Ser/Glu506Ala was mainly in a novel resting form to afford the absorption band at ca. 400. nm and an EPR signal with a highly anisotropic character derived from type III copper. However, Cys500Ser/Glu506Ala gave the same reaction intermediate (peroxide intermediate) as that from Cys500Ser and Cys500Ser/Glu506Gln. © 2015 Elsevier Inc.
Embargo Period 24 months
Journal
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- Journal of Inorganic Biochemistry
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Journal of Inorganic Biochemistry 149 88-90, 2015-08-01
Elsevier
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Keywords
Details 詳細情報について
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- CRID
- 1050845760872609024
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- NII Article ID
- 120005613973
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- NII Book ID
- AA00258264
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- ISSN
- 01620134
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- Web Site
- http://hdl.handle.net/2297/42216
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- Text Lang
- en
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- Article Type
- journal article
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- Data Source
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- IRDB
- CiNii Articles