The Crystal Structure of an Azide Complex of the Diferrous R2 Subunit of Ribonucleotide Reductase Displays a Novel Carboxylate Shift with Important Mechanistic Implications for Diiron-Catalyzed Oxygen Activation-Reference-Cited by-同舟云学术

The Crystal Structure of an Azide Complex of the Diferrous R2 Subunit of Ribonucleotide Reductase Displays a Novel Carboxylate Shift with Important Mechanistic Implications for Diiron-Catalyzed Oxygen Activation

Published:1999-03-01 Issue:11 Volume:121 Page:2346-2352
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Andersson Martin E.¹,Högbom Martin¹,Rinaldo-Matthis Agnes¹,Andersson K. Kristoffer¹,Sjöberg Britt-Marie¹,Nordlund Pär¹

Affiliation:

1. Contribution from the Department of Biochemistry, Stockholm University, S-106 91 Stockholm, Sweden, Department of Biochemistry, University of Oslo, P.O. Box 1041, Blindern, N-0316 Oslo, Norway, and Department of Molecular Biology, Stockholm University, S-106 91 Stockholm, Sweden

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja982280c

Reference61 articles.

1. Three-dimensional structure of the free radical protein of ribonucleotide reductase

2. Ribonucleotide reductases: radical enzymes with suicidal tendencies

3. Electron Paramagnetic Resonance and Nuclear Magnetic Resonance Studies of Class I Ribonucleotide Reductase

4. Carbon Dioxide Fixation Catalyzed By Metal Complexes

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