Evidence for a Di-μ-oxo Diamond Core in the Mn(IV)/Fe(IV) Activation Intermediate of Ribonucleotide Reductase from Chlamydia trachomatis-Reference-Cited by-同舟云学术

Evidence for a Di-μ-oxo Diamond Core in the Mn(IV)/Fe(IV) Activation Intermediate of Ribonucleotide Reductase from Chlamydia trachomatis

Published:2017-01-27 Issue:5 Volume:139 Page:1950-1957
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Martinie Ryan J.¹^ORCID,Blaesi Elizabeth J.¹,Krebs Carsten¹^ORCID,Bollinger J. Martin¹,Silakov Alexey¹,Pollock Christopher J.¹^ORCID

Affiliation:

1. Department of Chemistry and ‡Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, United States

Funder

Division of Graduate Education

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/jacs.6b11563

Reference89 articles.

1. Non-Heme Fe(IV)–Oxo Intermediates

2. The First Direct Characterization of a High-Valent Iron Intermediate in the Reaction of an α-Ketoglutarate-Dependent Dioxygenase: A High-Spin Fe(IV) Complex in Taurine/α-Ketoglutarate Dioxygenase (TauD) from Escherichia coli

3. Direct spectroscopic detection of a C-H-cleaving high-spin Fe(IV) complex in a prolyl-4-hydroxylase

4. Two interconverting Fe(IV) intermediates in aliphatic chlorination by the halogenase CytC3

5. Evidence that the Fosfomycin-Producing Epoxidase, HppE, Is a Non–Heme-Iron Peroxidase

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