Premium
The Structure of a Designed Diiron(III) Protein: Implications for Cofactor Stabilization and Catalysis
Author(s) -
Wade Herschel,
Stayrook Steven E.,
DeGrado William F.
Publication year - 2006
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200600042
Subject(s) - methane monooxygenase , cofactor , ribonucleotide reductase , chemistry , catalysis , stereochemistry , active site , hydrogen bond , crystal structure , ribonucleotide , reactivity (psychology) , oxidoreductase , enzyme , crystallography , biochemistry , molecule , organic chemistry , nucleotide , medicine , alternative medicine , pathology , protein subunit , gene
A closer look into the function of diiron proteins, such as methane monooxygenase and ribonucleotide reductase, is provided by the crystal structure of a designed diiron protein (the picture shows the Fe environment). Cofactor rigidity may be a factor in O 2 reactivity and a possible role of HisC ε H⋅⋅⋅O hydrogen bonds in cofactor stabilization is implicated.