Heme-Coordinating Inhibitors of Neuronal Nitric Oxide Synthase. Iron−Thioether Coordination Is Stabilized by Hydrophobic Contacts without Increased Inhibitor Potency-Reference-Cited by-同舟云学术

Heme-Coordinating Inhibitors of Neuronal Nitric Oxide Synthase. Iron−Thioether Coordination Is Stabilized by Hydrophobic Contacts without Increased Inhibitor Potency

Published:2009-12-16 Issue:2 Volume:132 Page:798-806
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Martell Jeffrey D.¹,Li Huiying¹,Doukov Tzanko¹,Martásek Pavel¹,Roman Linda J.¹,Soltis Michael¹,Poulos Thomas L.¹,Silverman Richard B.¹

Affiliation:

1. Departments of Chemistry and of Biochemistry, Molecular Biology, and Cell Biology, Center for Molecular Innovation and Drug Discovery, and Chemistry of Life Processes Institute, Northwestern University, Evanston, Illinois 60208-3113, Departments of Molecular Biology and Biochemistry, of Pharmaceutical Chemistry, and of Chemistry, University of California, Irvine, California 92697-3900, Macromolecular Crystallographic Group, Stanford Synchrotron Radiation Lightsource, SLAC, Stanford University, Stanford,...

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja908544f

Reference59 articles.

1. Effects of Ligation and Folding on Reduction Potentials of Heme Proteins

2. Spectroscopic Characterization of Five- and Six-Coordinate Ferrous−NO Heme Complexes. Evidence for Heme Fe−Proximal Cysteinate Bond Cleavage in the Ferrous−NO Adducts of the Trp-409Tyr/Phe Proximal Environment Mutants of Neuronal Nitric Oxide Synthase

3. Heme axial methionine fluxionality in Hydrogenobacter thermophilus cytochrome c552

4. Coordination chemistry of thioethers, selenoethers, and telluroethers in transition-metal complexes

5. Comparative NMR studies of cytochrome c and its active site octapeptide

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