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As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website.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

A molecular basis for no selectivity in soluble guanylate cyclase

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

Overview

authors

  • Boon, E. M.
  • Huang, S. H.
  • Marletta, Michael

publication date

  • June 2005

journal

  • Nature Chemical Biology  Journal

abstract

  • Soluble guanylate cyclases (sGCs) function as heme sensors that selectively bind nitric oxide (NO), triggering reactions essential to animal physiology. Recent discoveries place sGCs in the H-NOX family (heme nitric oxide/oxygen-binding domain), which includes bacterial proteins from aerobic and anaerobic organisms. Some H-NOX proteins tightly bind oxygen (O2), whereas others show no measurable affinity for O2, providing the basis for selective NO signaling in aerobic cells. Using a series of wild-type and mutant H-NOXs, we established a molecular basis for ligand discrimination. A distal pocket tyrosine is requisite for O2 binding in the H-NOX family. These data suggest that sGC uses a kinetic selection against O2; we propose that the O2 dissociation rate in the absence of this tyrosine is fast and that a stable O2 complex does not form.

subject areas

  • Amino Acid Sequence
  • Animals
  • Bacterial Proteins
  • Binding, Competitive
  • Biosensing Techniques
  • Guanylate Cyclase
  • Hemeproteins
  • Ligands
  • Molecular Sequence Data
  • Nitric Oxide
  • Oxygen
  • Protein Conformation
  • Receptors, Cytoplasmic and Nuclear
  • Sequence Alignment
  • Thermoanaerobacterium
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 1552-4450

Digital Object Identifier (DOI)

  • 10.1038/nchembio704

PubMed ID

  • 16407994
scroll to property group menus

Additional Document Info

start page

  • 53

end page

  • 59

volume

  • 1

issue

  • 1

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

  • About
  • Contact Us
  • Support