Active-Site Models of Bacterial Nitric Oxide Reductase Featuring Tris-Histidyl and Glutamic Acid Mimics: Influence of a Carboxylate Ligand on FeB Binding and the Heme Fe/FeB Redox Potential-Reference-Cited by-同舟云学术

Active-Site Models of Bacterial Nitric Oxide Reductase Featuring Tris-Histidyl and Glutamic Acid Mimics: Influence of a Carboxylate Ligand on FeB Binding and the Heme Fe/FeB Redox Potential

Published:2006-08-25 Issue:19 Volume:45 Page:7581-7583
ISSN:0020-1669
Container-title:Inorganic Chemistry
language:en
Short-container-title:Inorg. Chem.

Author:

Collman James P.¹,Yan Yi-Long¹,Lei Jianping¹,Dinolfo Peter H.¹

Affiliation:

1. Department of Chemistry, Stanford University, Stanford, California 94305-5080

Publisher

American Chemical Society (ACS)

Subject

Inorganic Chemistry,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/ic0609150

Reference25 articles.

1. Nitric Oxide in Biological Denitrification: Fe/Cu Metalloenzyme and Metal Complex NOx Redox Chemistry

2. The Active Site of the Bacterial Nitric Oxide Reductase Is a Dinuclear Iron Center

3. Two Conserved Glutamates in the Bacterial Nitric Oxide Reductase Are Essential for Activity but Not Assembly of the Enzyme

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