ArticleThe Journal of biological chemistry2008
Structure and ligand selection of hemoglobin II from Lucina pectinata.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed.
- Article
- Fluoride binding to characteristic heme-pocket centers: Insights into ligand stability.Journal of inorganic biochemistry · 2021Article
- Article
- The symbiotic 'all-rounders': Partnerships between marine animals and chemosynthetic nitrogen-fixing bacteria.Applied and environmental microbiology · 2021Review
- Host-Endosymbiont Genome Integration in a Deep-Sea Chemosymbiotic Clam.Molecular biology and evolution · 2021Article
- Lucina pectinata oxyhemoglobin (II-III) heterodimer pH susceptibility.Journal of inorganic biochemistry · 2020Article
- Chemical Biology of HChemical reviews · 2018Review
- Characterization and Expression of the Lucina pectinata Oxygen and Sulfide Binding Hemoglobin Genes.PloS one · 2016Article
- Tyrosine B10 triggers a heme propionate hydrogen bonding network loop with glutamine E7 moiety.Biochemical and biophysical research communications · 2012Article
- Degradation of sulfide by dehaloperoxidase-hemoglobin from Amphitrite ornata.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2011Article
- Structural determinants for the formation of sulfhemeprotein complexes.Biochemical and biophysical research communications · 2010Article
- Extreme differences between hemoglobins I and II of the clam Lucina pectinalis in their reactions with nitrite.Biochimica et biophysica acta · 2010Article
- Two-step counterdiffusion protocol for the crystallization of haemoglobin II from Lucina pectinata in the pH range 4-9.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
- Recombinant hemoglobin II from Lucina pectinata: a large-scale method for hemeprotein expression in E. coli.The protein journal · 2010Article
- Factors controlling the reactivity of hydrogen sulfide with hemeproteins.Biochemistry · 2009Article
- Crystallization and diffraction patterns of the oxy and cyano forms of the Lucina pectinata haemoglobins complex.Acta crystallographica. Section F, Structural biology and crystallization communications · 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.
Funding
Abstract
Lucina pectinata ctenidia harbor three heme proteins: sulfide-reactive hemoglobin I (HbI(Lp)) and the oxygen transporting hemoglobins II and III (HbII(Lp) and HbIII(Lp)) that remain unaffected by the presence of H(2)S. The mechanisms used by these three proteins for their function, including ligand control, remain unknown. The crystal structure of oxygen-bound HbII(Lp) shows a dimeric oxyHbII(Lp) where oxygen is tightly anchored to the heme through hydrogen bonds with Tyr(30)(B10) and Gln(65)(E7). The heme group is buried farther within HbII(Lp) than in HbI(Lp). The proximal His(97)(F8) is hydrogen bonded to a water molecule, which interacts electrostatically with a propionate group, resulting in a Fe-His vibration at 211 cm(-1). The combined effects of the HbII(Lp) small heme pocket, the hydrogen bonding network, the His(97) trans-effect, and the orientation of the oxygen molecule confer stability to the oxy-HbII(Lp) complex. Oxidation of HbI(Lp) Phe(B10) --> Tyr and HbII(Lp) only occurs when the pH is decreased from pH 7.5 to 5.0. Structural and resonance Raman spectroscopy studies suggest that HbII(Lp) oxygen binding and transport to the host bacteria may be regulated by the dynamic displacements of the Gln(65)(E7) and Tyr(30)(B10) pair toward the heme to protect it from changes in the heme oxidation state from Fe(II) to Fe(III).
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.