ArticleProceedings of the National Academy of Sciences of the United States of America2004
Crystal structure of an oxygen-binding heme domain related to soluble guanylate cyclases.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 124 papers.
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Who cites it
124 citing papers in PubMed, 268 citations in OpenAlex.
- Benchmark Study for Calculations of pKa Values of Metal Ligands in Proteins.Journal of chemical theory and computation · 2026Article
- Bafilomycin A1 is a promising therapeutic agent against T. spiralis infection by inhibiting the heme-transporting ATP6V0C/HRG-1 complex.PLoS pathogens · 2026Article
- Oxidative Activation of the Heme Nitric Oxide/Oxygen-Binding Protein (H-NOX) fromBiochemistry · 2025Article
- The direct expression of apo heme proteins: A general strategy to obtain designer heme proteins with abiological cofactors.Methods in enzymology · 2025Article
- The H-NOX protein structure adapts to different mechanisms in sensors interacting with nitric oxide.Chemical science · 2023Article
- Gas and light: triggers of c-di-GMP-mediated regulation.FEMS microbiology reviews · 2023Review
- Backbone and side chain NMR assignment of the heme-nitric oxide/oxygen binding (H-NOX) domain from Nostoc punctiforme.Biomolecular NMR assignments · 2022Article
- Sensory Perception in Bacterial Cyclic Diguanylate Signal Transduction.Journal of bacteriology · 2022Review
- H-NOX proteins in the virulence of pathogenic bacteria.Bioscience reports · 2022Review
- Soluble guanylyl cyclase: Molecular basis for ligand selectivity and actionFrontiers in molecular biosciences · 2022Review
- Endogenous Hemoprotein-Dependent Signaling Pathways of Nitric Oxide and Nitrite.Inorganic chemistry · 2021Review
- Structural Perspectives on the Mechanism of Soluble Guanylate Cyclase Activation.International journal of molecular sciences · 2021Review
- Ultrafast dynamics of heme distortion in the OCommunications chemistry · 2021Article
- Corrole-Substituted Fluorescent Heme Proteins.Inorganic chemistry · 2021Article
- Solution structures of the Shewanella woodyi H-NOX protein in the presence and absence of soluble guanylyl cyclase stimulator IWP-051.Protein science : a publication of the Protein Society · 2021Article
- A new paradigm for gaseous ligand selectivity of hemoproteins highlighted by soluble guanylate cyclase.Journal of inorganic biochemistry · 2021Review
- Computational Identification of Functional Centers in Complex Proteins: A Step-by-Step Guide With Examples.Frontiers in bioinformatics · 2021Article
- Recent evidence for multifactorial biofilm regulation by heme sensor proteins NosP and H-NOX.Chemistry letters · 2021Article
- Gas Sensing by Bacterial H-NOX Proteins: An MD Study.Molecules (Basel, Switzerland) · 2020Article
- Structural insights into the mechanism of oxidative activation of heme-free H-NOX from Vibrio cholerae.The Biochemical journal · 2020Article
64 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Soluble guanylate cyclases are nitric oxide-responsive signaling proteins in which the nitric oxide sensor is a heme-binding domain of unknown structure that we have termed the heme-NO and oxygen binding (H-NOX) domain. H-NOX domains are also found in bacteria, either as isolated domains, or are fused through a membrane-spanning region to methyl-accepting chemotaxis proteins. We have determined the crystal structure of an oxygen-binding H-NOX domain of one such signaling protein from the obligate anaerobe Thermoanaerobacter tengcongensis at 1.77-angstroms resolution, revealing a protein fold unrelated to known structures. Particularly striking is the structure of the protoporphyrin IX group, which is distorted from planarity to an extent not seen before in protein-bound heme groups. Comparison of the structure of the H-NOX domain in two different crystal forms suggests a mechanism whereby alteration in the degree of distortion of the heme group is coupled to changes on the molecular surface of the H-NOX domain and potentially to changes in intermolecular interactions.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.