Kinetic and paramagnetic NMR investigations of the inhibition of Streptomyces antibioticus tyrosinase-Reference-Cited by-同舟云学术

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Kinetic and paramagnetic NMR investigations of the inhibition of Streptomyces antibioticus tyrosinase

Published:2000-01 Issue:1-3 Volume:8 Page:27-35
ISSN:1381-1177
Container-title:Journal of Molecular Catalysis B: Enzymatic
language:en
Short-container-title:Journal of Molecular Catalysis B: Enzymatic

Author:

Bubacco Luigi,Vijgenboom Erik,Gobin Christine,Tepper Armand W.J.W.,Salgado Jesús,Canters Gerard W.

Publisher

Elsevier BV

Subject

Process Chemistry and Technology,Biochemistry,Bioengineering,Catalysis

Reference28 articles.

1. Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2 Å resolution

2. Crystal structure of deoxygenatedlimulus polyphemussubunit II hemocyanin at 2.18 Å resolution: Clues for a mechanism for allosteric regulation

3. Crystal structure of a functional unit from Octopus hemocyanin

4. Different origins of metal binding sites in binuclear copper proteins, tyrosinase and hemocyanin

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3. The Novel Role of Tyrosinase Enzymes in the Storage of Globally Significant Amounts of Carbon in Wetland Ecosystems;Environmental Science & Technology;2022-08-09

4. Expression, Purification, and Characterization of a Well-Adapted Tyrosinase from Peatlands Identified by Partial Community Analysis;Environmental Science & Technology;2021-06-22

5. Ditopic Chelators of Dicopper Centers for Enhanced Tyrosinases Inhibition;Chemistry – A European Journal;2021-02

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