Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

Biochemistry of soluble guanylate cyclase

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Derbyshire, E. R.
  • Marletta, Michael

publication date

  • 2009

journal

  • Handbook of Experimental Pharmacology  Journal

abstract

  • Nitric oxide (NO) functions in biology as both a critical cytotoxic agent and an essential signaling molecule. The toxicity of the diatomic gas has long been accepted; however, it was not known to be a signaling molecule until it was identified as the endothelium-derived relaxing factor (EDRF). Since this discovery, the physiological signaling pathways that are regulated by NO have been the focus of numerous studies. Many of the cellular responses that NO modulates are mediated by the heme protein soluble guanylate cyclase (sGC). NO binds to sGC at a diffusion controlled rate, and leads to a several 100-fold increase in the synthesis of the second messenger cGMP from GTP. Other diatomic gases either do not bind (dioxygen), or do not significantly activate (carbon monoxide) sGC. This provides selectivity and efficiency for NO even in an aerobic environment, which is critical due to the high reactivity of NO. Several biochemical studies have focused on elucidating the mechanism of NO activation and O(2) discrimination. Significant advances in our understanding of these topics have occurred with the identification and characterization of the sGC-like homologues termed Heme-Nitric oxide and OXygen binding (H-NOX) proteins.

subject areas

  • Animals
  • Cyclic GMP
  • Guanylate Cyclase
  • Hemeproteins
  • Humans
  • Ligands
  • Nitric Oxide
  • Oxygen
  • Protein Binding
  • Protein Isoforms
  • Receptors, Cytoplasmic and Nuclear
  • Signal Transduction
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 978-3-540-68960-7

Digital Object Identifier (DOI)

  • 10.1007/978-3-540-68964-5_2

PubMed ID

  • 19089323
scroll to property group menus

Additional Document Info

start page

  • 17

end page

  • 31

volume

  • 191

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support