Electron Paramagnetic Resonance Spectroscopy of the Heme Domain of Inducible Nitric Oxide Synthase: Binding of Ligands at the Arginine Site Induces Changes in the Heme Ligation Geometry-Reference-Cited by-同舟云学术

Electron Paramagnetic Resonance Spectroscopy of the Heme Domain of Inducible Nitric Oxide Synthase: Binding of Ligands at the Arginine Site Induces Changes in the Heme Ligation Geometry

Published:1996-01-01 Issue:24 Volume:35 Page:7626-7630
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Salerno John C.¹,Martasek Pavel¹,Roman Linda J.¹,Masters Bettie Sue S.¹

Affiliation:

1. Rensselaer Polytechnic Institute, 15th Street, Troy, New York 12180, and The University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, Texas 78284-7760

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi960607l

Reference25 articles.

1. Nitric oxide synthase regulatory sites. Phosphorylation by cyclic AMP-dependent protein kinase, protein kinase C, and calcium/calmodulin protein kinase; identification of flavin and calmodulin binding sites.

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