ArticleBiochemistry2014
Fluctuations of an exposed π-helix involved in lipoxygenase substrate recognition.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- Description of the rate-limiting hydrogen tunneling mechanism for plant 9- and 13-lipoxygenases.Protein science : a publication of the Protein Society · 2026Article
- Computational Method for the Detection of Communication Pathways in Enzymes that Correlate with Experimentally Defined Thermal Activation Networks.The journal of physical chemistry letters · 2026Article
- Impact ofBiochemistry · 2024Article
- Plastidic membrane lipids are oxidized by a lipoxygenase inFrontiers in plant science · 2022Article
- Fatty Acid Allosteric Regulation of C-H Activation in Plant and Animal Lipoxygenases.Molecules (Basel, Switzerland) · 2020Review
- EPR Spectroscopic Studies of Lipoxygenases.Chemistry, an Asian journal · 2020Review
- Comparative kinetic isotope effects on first- and second-order rate constants of soybean lipoxygenase variants uncover a substrate-binding network.The Journal of biological chemistry · 2019Article
- An ensemble of lipoxygenase structures reveals novel conformations of the Fe coordination sphere.Protein science : a publication of the Protein Society · 2019Article
- Site-directed spin label electron paramagnetic resonance spectroscopy as a probe of conformational dynamics in the Fe(III) "locked-off" state of the CO-sensing transcription factor CooA.Protein science : a publication of the Protein Society · 2018Article
- Ferrochelatase π-helix: Implications from examining the role of the conserved π-helix glutamates in porphyrin metalation and product release.Archives of biochemistry and biophysics · 2018Article
- The structural basis for specificity in lipoxygenase catalysis.Protein science : a publication of the Protein Society · 2015Review
- Connecting lipoxygenase function to structure by electron paramagnetic resonance.Accounts of chemical research · 2014Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The second helix in lipoxygenases adapts to permit substrate access to the active site, but details of this process are varied and poorly understood. We therefore examined the dynamics of helix 2 in solutions of spin-labeled soybean lipoxygenase-1 and spin relaxation at 60 K of the spin-labels by catalytic iron. Helix 2 in soybean lipoxygenase structures is surface-exposed and contains one turn of π-helix, centrally located. A site-directed spin-label scan of 18 of the 21 helix 2 residues, and electron paramagnetic resonance, showed that the π-helical segment became unusually mobile, on a nanosecond time scale, under conditions favoring substrate binding (pH 9 and lipid addition), while segments before and after had relatively unchanged dynamics. Backbone dynamics of residues in the π-helical segment appeared to be correlated, at pH 9. Samples also were frozen to examine the polarity and proticity of the local environments, the effect of the local environment on intrinsic relaxation, and dipolar relaxation by two symmetries of catalytic iron. The average hyperfine tensor component, Azz, of four π-helix residues decreased by 1.75 G, with an increase in pH from 7 to 9, while it remained unaffected for nearby buried residues. Power saturation data suggested the change in polarity specific to the π-helix altered the intrinsic relaxation rates. Different symmetries of iron contributed to distance-dependent magnetic relaxation. We interpret these data to mean that a π-helix in the second helix of plant lipoxygenases is highly dynamic and is the site where lipid chains penetrate to inner helices that outline the substrate pocket.
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