The structure of a designed diiron(III) protein: Implications for cofactor stabilization and catalysis

Herschel Wade, Steven E. Stayrook, William F. DeGrado

Research output: Contribution to journalArticlepeer-review

Abstract

(Chemical Equation Presented) 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 O2 reactivity and a possible role of HisCεH⋯O hydrogen bonds in cofactor stabilization is implicated.

Original languageEnglish (US)
Pages (from-to)4951-4954
Number of pages4
JournalAngewandte Chemie - International Edition
Volume45
Issue number30
DOIs
StatePublished - Jul 24 2006
Externally publishedYes

Keywords

  • Diiron enzymes
  • Metalloproteins
  • Protein models
  • Protein structures

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

Fingerprint

Dive into the research topics of 'The structure of a designed diiron(III) protein: Implications for cofactor stabilization and catalysis'. Together they form a unique fingerprint.

Cite this