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pro vyhledávání: '"Anthony J. Pastore"'
Publikováno v:
Journal of inorganic biochemistry. 234
Amicyanin is a type 1 copper protein with a single tryptophan residue. Using genetic code expansion, the tryptophan was selectively replaced with the unnatural amino acid, 5-hydroxytryptophan (5-HTP). The 5-HTP substituted amicyanin exhibited absorba
Autor:
Ruijie D. Teo, Matthew J. Burg, Steven D. Bruner, David N. Beratan, Alexander Angerhofer, Alvaro Montoya, Umar T. Twahir, Anthony J. Pastore
Publikováno v:
The Journal of Biological Chemistry
The hexameric low-pH stress response enzyme oxalate decarboxylase catalyzes the decarboxylation of the oxalate mono-anion in the soil bacterium Bacillus subtilis. A single protein subunit contains two Mn-binding cupin domains, and catalysis depends o
Publikováno v:
Arch Biochem Biophys
Oxo-bridged diiron proteins are a distinct class of non-heme iron proteins. Their active sites are composed of two irons that are coordinated by amino acid side chains, and a bridging oxygen that interacts with each iron. These proteins are members o