The Structure of a Designed Diiron(III) Protein: Implications for Cofactor Stabilization and Catalysis | Zendy

Wade Herschel | Zendy; Stayrook Steven E. | Zendy; DeGrado William F. | Zendy

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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.

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