Dicobalt II−II, II−III, and III−III Complexes as Spectroscopic Models for Dicobalt Enzyme Active Sites-Reference-Cited by-同舟云学术

Dicobalt II−II, II−III, and III−III Complexes as Spectroscopic Models for Dicobalt Enzyme Active Sites

Published:2008-05-22 Issue:12 Volume:47 Page:5079-5092
ISSN:0020-1669
Container-title:Inorganic Chemistry
language:en
Short-container-title:Inorg. Chem.

Author:

Johansson Frank B.¹,Bond Andrew D.¹,Nielsen Ulla Gro¹,Moubaraki Boujemaa¹,Murray Keith S.¹,Berry Kevin J.¹,Larrabee James A.¹,McKenzie Christine J.¹

Affiliation:

1. Department of Physics and Chemistry, University of Southern Denmark, Campusvej 55, 5230 Odense M, Denmark, School of Chemistry, Building 23, Monash University, Clayton, Victoria Australia, Department of Chemistry and Biochemistry, Middlebury College, Middlebury, Vermont, U.S.A., and Westernport Secondary College, Hastings, Victoria, 3915, Australia

Publisher

American Chemical Society (ACS)

Subject

Inorganic Chemistry,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/ic7020534

Reference60 articles.

1. Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme

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3. Insights into the Mechanism of Escherichia coli Methionine Aminopeptidase from the Structural Analysis of Reaction Products and Phosphorus-Based Transition-State Analogues,

4. Metalloaminopeptidases: Common Functional Themes in Disparate Structural Surroundings

5. Binuclear Metallohydrolases

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