ArticleJournal of the American Chemical Society2009
Effect of mutation of carboxyl side-chain amino acids near the heme on the midpoint potentials and ligand binding constants of nitrophorin 2 and its NO, histamine, and imidazole complexes.
Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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
13 citing papers in PubMed, 32 citations in OpenAlex.
- Nitric oxide delivery and heme-assisted S-nitrosation by the bedbug nitrophorin.Journal of inorganic biochemistry · 2023Article
- Controlling a burn: outer-sphere gating of hydroxylamine oxidation by a distal base in cytochrome P460.Chemical science · 2019Article
- Structure and Activation of Soluble Guanylyl Cyclase, the Nitric Oxide Sensor.Antioxidants & redox signaling · 2017Review
- NMR investigations of nitrophorin 2 belt side chain effects on heme orientation and seating of native N-terminus NP2 and NP2(D1A).Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- NMR studies of the dynamics of nitrophorin 2 bound to nitric oxide.Biochemistry · 2013Article
- Structure and ligand-binding properties of the biogenic amine-binding protein from the saliva of a blood-feeding insect vector of Trypanosoma cruzi.Acta crystallographica. Section D, Biological crystallography · 2013Article
- Native N-terminus nitrophorin 2 from the kissing bug: similarities to and differences from NP2(D1A).Chemistry & biodiversity · 2012Article
- Nuclear inelastic scattering and Mössbauer spectroscopy as local probes for ligand binding modes and electronic properties in proteins: vibrational behavior of a ferriheme center inside a β-barrel protein.Journal of the American Chemical Society · 2012Article
- pH-Dependent conformational changes in proteins and their effect on experimental pK(a)s: the case of Nitrophorin 4.PLoS computational biology · 2012Article
- NMR studies of nitrophorin distal pocket side chain effects on the heme orientation and seating of NP2 as compared to NP1.Journal of inorganic biochemistry · 2011Article
- Oxidation and loss of heme in soluble guanylyl cyclase from Manduca sexta.Biochemistry · 2011Article
- Structure and mechanism in salivary proteins from blood-feeding arthropods.Toxicon : official journal of the International Society on Toxinology · 2010Review
- 1H and 13C NMR spectroscopic studies of the ferriheme resonances of three low-spin complexes of wild-type nitrophorin 2 and nitrophorin 2(V24E) as a function of pH.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Nitrophorins (NPs) are a group of NO-carrying heme proteins found in the saliva of a blood-sucking insect from tropical Central and South America, Rhodnius prolixus, the "kissing bug". NO is kept stable for long periods of time by binding it as an axial ligand to a ferriheme center. The fact that the nitrophorins are stabilized as Fe(III)-NO proteins is a unique property because most heme proteins are readily autoreduced by excess NO and bind NO to the Fe(II) heme irreversibly (K(d)s in the picomolar range). In contrast, the nitrophorins, as Fe(III) heme centers, have K(d)s in the micromolar to nanomolar range and thus allow NO to dissociate upon dilution following injection into the tissues of the victim. This NO can cause vasodilation and thereby allow more blood to be transported to the site of the wound. We prepared 13 site-directed mutants of three major nitrophorins, NP2, NP1, and NP4, to investigate the stabilization of the ferric-NO heme center and preservation of reversible binding that facilitates these proteins' NO storage, transport, and release functions. Of the mutations in which Glu and/or Asp were replaced by Ala, most of these carboxyls show a significant role stabilizing Fe(III)-NO over Fe(II)-NO, with buried E53 of NP2 or E55 of NP1 and NP4 being the most important and partially buried D29 of NP2 or D30 of NP4 being second in importance. The pK(a)s of the carboxyl groups studied vary significantly but all are largely deprotonated at pH 7.5 except E124.
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.