ArticleProceedings of the National Academy of Sciences of the United States of America2014
Structural insights into the role of iron-histidine bond cleavage in nitric oxide-induced activation of H-NOX gas sensor proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
52 citing papers in PubMed, 96 citations in OpenAlex.
- Article
- Structure and function of persulfide dioxygenase fromiScience · 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
- Conformation-Dependent Hydrogen-Bonding Interactions in a Switchable Artificial Metalloprotein.Biochemistry · 2024Article
- Nitric Oxide Binding Geometry in Heme-Proteins: Relevance for Signal Transduction.Antioxidants (Basel, Switzerland) · 2024Review
- Metalloprotein enabled redox signal transduction in microbes.Current opinion in chemical biology · 2023Review
- NosP Detection of Heme ModulatesBiochemistry · 2023Article
- 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
- H-NOX Regulates Biofilm Formation inBiochemistry · 2023Article
- Cellular Factors That Shape the Activity or Function of Nitric Oxide-Stimulated Soluble Guanylyl Cyclase.Cells · 2023Review
- Backbone and side chain NMR assignment of the heme-nitric oxide/oxygen binding (H-NOX) domain from Nostoc punctiforme.Biomolecular NMR assignments · 2022Article
- The Mechanism of Biochemical NO-Sensing: Insights from Computational Chemistry.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Corrole-protein interactions in H-NOX and HasA.RSC chemical biology · 2022Article
- Soluble guanylyl cyclase: Molecular basis for ligand selectivity and actionFrontiers in molecular biosciences · 2022Review
- Designer Heme Proteins: Achieving Novel Function with Abiological Heme Analogues.Accounts of chemical research · 2021Article
- Characterization of a Cobalt-Substituted Globin-Coupled Oxygen Sensor Histidine Kinase fromACS omega · 2021Article
- Insights into the ObservedACS omega · 2021Article
- Structural Perspectives on the Mechanism of Soluble Guanylate Cyclase Activation.International journal of molecular sciences · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Heme-nitric oxide/oxygen (H-NOX) binding domains are a recently discovered family of heme-based gas sensor proteins that are conserved across eukaryotes and bacteria. Nitric oxide (NO) binding to the heme cofactor of H-NOX proteins has been implicated as a regulatory mechanism for processes ranging from vasodilation in mammals to communal behavior in bacteria. A key molecular event during NO-dependent activation of H-NOX proteins is rupture of the heme-histidine bond and formation of a five-coordinate nitrosyl complex. Although extensive biochemical studies have provided insight into the NO activation mechanism, precise molecular-level details have remained elusive. In the present study, high-resolution crystal structures of the H-NOX protein from Shewanella oneidensis in the unligated, intermediate six-coordinate and activated five-coordinate, NO-bound states are reported. From these structures, it is evident that several structural features in the heme pocket of the unligated protein function to maintain the heme distorted from planarity. NO-induced scission of the iron-histidine bond triggers structural rearrangements in the heme pocket that permit the heme to relax toward planarity, yielding the signaling-competent NO-bound conformation. Here, we also provide characterization of a nonheme metal coordination site occupied by zinc in an H-NOX protein.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.