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

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

doi:10.1002/anie.200600042

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 journal › Article › peer-review

31 Scopus citations

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 HisC^εH⋯O hydrogen bonds in cofactor stabilization is implicated.

Original language	English (US)
Pages (from-to)	4951-4954
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	45
Issue number	30
DOIs	https://doi.org/10.1002/anie.200600042
State	Published - Jul 24 2006
Externally published	Yes

Keywords

Diiron enzymes
Metalloproteins
Protein models
Protein structures

ASJC Scopus subject areas

Catalysis
Chemistry(all)

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10.1002/anie.200600042

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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.",

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AU - DeGrado, William F.

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AB - (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.

KW - Diiron enzymes

KW - Metalloproteins

KW - Protein models

KW - Protein structures

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

Abstract

Keywords

ASJC Scopus subject areas

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