The sole tryptophan of amicyanin enhances its thermal stability but does not influence the electronic properties of the type 1 copper site
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference59 articles.
1. Cupredoxins—A study of how proteins may evolve to use metals for bioenergetic processes
2. Investigating the structure and function of cupredoxins
3. Electronic Structures of Metal Sites in Proteins and Models: Contributions to Function in Blue Copper Proteins
4. X-ray Structure of the Cupredoxin Amicyanin, fromParacoccus denitrificans, Refined at 1.31 Å Resolution
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1. Substitution of the sole tryptophan of the cupredoxin, amicyanin, with 5-hydroxytryptophan alters fluorescence properties and energy transfer to the type 1 copper site;Journal of Inorganic Biochemistry;2022-09
2. Metalloprotein catalysis: structural and mechanistic insights into oxidoreductases from neutron protein crystallography;Acta Crystallographica Section D Structural Biology;2021-09-27
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4. Cu in biology: Unleashed by O2 and now irreplaceable;Inorganica Chimica Acta;2018-09
5. Relaxation of structural constraints during Amicyanin unfolding;Journal of Inorganic Biochemistry;2018-02
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