ReviewScientifica2012
Hemoglobin: a nitric-oxide dioxygenase.
Review in Scientifica, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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
23 citing papers in PubMed, 77 citations in OpenAlex.
- From Transient to Metastable: Generation, Characterization, and Biomimetic Reactivity Studies of Well-Defined Heme Peroxynitrite Model Systems.Journal of the American Chemical Society · 2025Article
- Hemoglobin as an oxygen gasoreceptor.Acta biochimica Polonica · 2025Review
- Vibrational analyses of the reaction of oxymyoglobin with NO using a photolabile caged NO donor at cryogenic temperatures.Journal of inorganic biochemistry · 2024Article
- Transcriptomic profiling of haloarchaeal denitrification through RNA-Seq analysis.Applied and environmental microbiology · 2024Article
- Ordered Motions in the Nitric-Oxide Dioxygenase Mechanism of Flavohemoglobin and Assorted Globins with Tightly Coupled Reductases.Advances in experimental medicine and biology · 2023Article
- Carbon Monoxide and Nitric Oxide as Examples of the Youngest Class of Transmitters.International journal of molecular sciences · 2021Review
- Quantitative Modeling Extends the Antibacterial Activity of Nitric Oxide.Frontiers in physiology · 2020Article
- Characterization of a thaumarchaeal symbiont that drives incomplete nitrification in the tropical sponge Ianthella basta.Environmental microbiology · 2019Article
- Reporter Cell Assessment of TLR4-Induced NF-κB Responses to Cell-Free Hemoglobin and the Influence of Biliverdin.Biomedicines · 2019Article
- Replacement of the Distal Histidine Reveals a Noncanonical Heme Binding Site in a 2-on-2 Hemoglobin.Biochemistry · 2018Article
- Distinct Nitrite and Nitric Oxide Physiologies in Escherichia coli and Shewanella oneidensis.Applied and environmental microbiology · 2018Article
- Covalent attachment of the heme to Synechococcus hemoglobin alters its reactivity toward nitric oxide.Journal of inorganic biochemistry · 2017Article
- Cytoglobin regulates blood pressure and vascular tone through nitric oxide metabolism in the vascular wall.Nature communications · 2017Article
- The influence of haemoglobin and iron on in vitro mycobacterial growth inhibition assays.Scientific reports · 2017Article
- Characterization of the Heme Pocket Structure and Ligand Binding Kinetics of Non-symbiotic Hemoglobins from the Model LegumeFrontiers in plant science · 2017Article
- Discovery and dissection of metabolic oscillations in the microaerobic nitric oxide response network of Escherichia coli.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Globins Scavenge Sulfur Trioxide Anion Radical.The Journal of biological chemistry · 2015Article
- Extracellular hemoglobin: the case of a friend turned foe.Frontiers in physiology · 2015Review
- Characterization of THB1, a Chlamydomonas reinhardtii truncated hemoglobin: linkage to nitrogen metabolism and identification of lysine as the distal heme ligand.Biochemistry · 2014Article
- The McClure and Weiss models of Fe-O2 bonding for oxyhemes, and the HbO2 + NO reaction.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
Abstract
Members of the hemoglobin superfamily efficiently catalyze nitric-oxide dioxygenation, and when paired with native electron donors, function as NO dioxygenases (NODs). Indeed, the NOD function has emerged as a more common and ancient function than the well-known role in O2 transport-storage. Novel hemoglobins possessing a NOD function continue to be discovered in diverse life forms. Unique hemoglobin structures evolved, in part, for catalysis with different electron donors. The mechanism of NOD catalysis by representative single domain hemoglobins and multidomain flavohemoglobin occurs through a multistep mechanism involving O2 migration to the heme pocket, O2 binding-reduction, NO migration, radical-radical coupling, O-atom rearrangement, nitrate release, and heme iron re-reduction. Unraveling the physiological functions of multiple NODs with varying expression in organisms and the complexity of NO as both a poison and signaling molecule remain grand challenges for the NO field. NOD knockout organisms and cells expressing recombinant NODs are helping to advance our understanding of NO actions in microbial infection, plant senescence, cancer, mitochondrial function, iron metabolism, and tissue O2 homeostasis. NOD inhibitors are being pursued for therapeutic applications as antibiotics and antitumor agents. Transgenic NOD-expressing plants, fish, algae, and microbes are being developed for agriculture, aquaculture, and industry.
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.