ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2009
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.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 25 citations in OpenAlex.
- Influence of heme c attachment on heme conformation and potential.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Electrostatic Tuning of the Ligand Binding Mechanism by Glu27 in Nitrophorin 7.Scientific reports · 2018Article
- Dimerization of nitrophorin 4 at low pH and comparison to the K1A mutant of nitrophorin 1.Biochemistry · 2015Article
- Structure and dynamics of the membrane attaching nitric oxide transporter nitrophorin 7.F1000Research · 2015Article
- 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
- Inactivation of the heme degrading enzyme IsdI by an active site substitution that diminishes heme ruffling.The Journal of biological chemistry · 2012Article
- Native N-terminus nitrophorin 2 from the kissing bug: similarities to and differences from NP2(D1A).Chemistry & biodiversity · 2012Article
- Assignment of the 1H NMR resonances of protein residues in close proximity to the heme of the nitrophorins: similarities and differences among the four proteins from the saliva of the adult blood-sucking insect Rhodnius prolixus.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 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
- Crystallization and preliminary X-ray crystallographic analysis of the membrane-binding haemprotein nitrophorin 7 from Rhodnius prolixus.Acta crystallographica. Section F, Structural biology and crystallization communications · 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
- Linear correlation between 1H and 13C chemical shifts of ferriheme proteins and model ferrihemes.Inorganic chemistry · 2011Article
- NMR and DFT investigation of heme ruffling: functional implications for cytochrome c.Journal of the American Chemical Society · 2010Article
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6 authors at 2 institutions in 2 countries.
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Abstract
The ferriheme resonances of the low-spin (S = 1/2) complexes of wild-type (wt) nitrophorin 2 (NP2) and its heme pocket mutant NP2(V24E) with imidazole (ImH), histamine (Hm), and cyanide (CN(-)) as the sixth ligand have been investigated by NMR spectroscopy as a function of pH (4.0-7.5). For the three wt NP2 complexes, the ratio of the two possible heme orientational isomers, A and B, remains almost unchanged (ratio of A:B approximately 1:6 to 1:5) over this wide pH range. However, strong chemical exchange cross peaks appear in the nuclear Overhauser effect spectroscopy/exchange spectroscopy (NOESY/EXSY) spectra for the heme methyl resonances at low pH (pH* 4.0-5.5), which indicate chemical exchange between two species. We have shown these to be two different exogenous ImH or Hm orientations that are denoted B and B', with the ImH plane nearly parallel and perpendicular to the ImH plane of the protein-provided His57, respectively. The wt NP2-CN complex also shows EXSY cross peaks due to chemical exchange, which is shown to be a result of interchange between two ruffling distortions of the heme. The same ruffling distortion interchange is also responsible for the ImH and Hm chemical exchange. For the three NP2(V24E) ligand complexes, no EXSY cross peaks are observed, but the A:B ratios change dramatically with pH. The fact that heme favors the A orientation highly for NP2(V24E) at low pH as compared with wt NP2 is believed to be due to the steric effect of the V24E mutation. The existence of the B' species at lower pH for wt NP2 complexes and the increase in A heme orientation at lower pH for NP2(V24E) are believed to be a result of a change in structure near Glu53 when it is protonated at low pH. 1H{13C} heteronuclear multiple quantum coherence (HMQC) spectra are very helpful for the assignment of heme and nearby protein side chain resonances.
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