Proton NMR study of myoglobin reconstituted with 3,7-diethyl-2,8-dimethyl iron porphyrin: Remarkable influence of peripheral substitution on heme rotation

Juillard, Sandrine; Bondon, Arnaud; Simonneaux, Gérard

doi:10.1016/j.jinorgbio.2006.04.005

Cited by 5 publications

(4 citation statements)

References 27 publications

(27 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It is important to note in the scheme of Figure 4B that the direct 360° rotation is not involved, and that rotation occurs in a stepwise manner. This scheme is consistent with the clever NMR experiments reported by the group of Simonneaux [17,18]. They reconstituted Mb with small hemes of 3,7-diethyl-2,8-dimethylhemin and 3-ethyl-2-methylhemin.…”

Section: Heme Rotation In Myoglobinsupporting

confidence: 90%

Dynamic Motion and Rearranged Molecular Shape of Heme in Myoglobin: Structural and Functional Consequences

Neya

2013

Molecules

View full text Add to dashboard Cite

Myoglobin, a simple oxygen binding protein, was reconstituted with various types of synthetic hemes to manipulate the heme-globin interactions. From the paramagnetic NMR analysis, small heme was found to rotate rapidly about the iron-histidine bond upon. This is a novel and typical example for the fluctuation of protein. The dynamic NMR analysis indicated that the 360° rotational rate of a small heme was 1,400 s −1 at room temperature. The X-ray analyses revealed that the tertiary structure of globin containing the smallest heme was closely similar to that of native protein despite extensive destruction of the specific heme-globin interactions. The functional analyses of O 2 binding showed that the loose heme-globin contacts do not significantly affect the oxygen binding. On the other hand, the rearrangement of tetrapyrrole array and the non-planar deformation in porphyrin ring significantly affect the functional properties of myoglobin. These results, taken together, indicate that the essential factors to regulate the myoglobin function are hidden under the molecular shape of prosthetic group rather than in the nonbonded heme-globin contacts.

show abstract

Section: Heme Rotation In Myoglobinsupporting

confidence: 90%

Dynamic Motion and Rearranged Molecular Shape of Heme in Myoglobin: Structural and Functional Consequences

Neya

2013

Molecules

View full text Add to dashboard Cite

show abstract

“…5 and 6 . Mb and Hb are the model system for protein folding 52 53 54 55 56 . For Hb NMR, we observed the peaks for Leu28β, Val17α (γCH 3 ) Val17α (βCH 3 ), Phe98α (ζCH), Tyr24α (δCH 2 ), HIS:Hα, Phe98α (δCH 2 ) and Tyr24α (εCH 2 ) appeared at −0.81, 0.44, 1.55, 5.88, 6.19, 6.84, 7.65 and7.78 ppm in case of the Air plasma but disappeared in case of the Ar and N 2 plasma.…”

Section: Resultsmentioning

confidence: 99%

Influence of reactive species on the modification of biomolecules generated from the soft plasma

Attri

Kumar

Park

et al. 2015

Sci Rep

107

View full text Add to dashboard Cite

Plasma medicine is an upcoming research area that has attracted the scientists to explore more deeply the utility of plasma. So, apart from the treating biomaterials and tissues with plasma, we have studied the effect of soft plasma with different feeding gases such as Air, N2 and Ar on modification of biomolecules. Hence, in this work we have used the soft plasma on biomolecules such as proteins ((Hemoglobin (Hb) and Myoglobin (Mb)), calf thymus DNA and amino acids. The structural changes or structural modification of proteins and DNA have been studied using circular dichroism (CD), fluorescence spectroscopy, protein oxidation test, gel electrophoresis, UV-vis spectroscopy, dynamic light scattering (DLS) and 1D NMR, while Liquid Chromatograph/Capillary Electrophoresis-Mass Spectrometer (LC/CE-MS) based on qualitative and quantitative bio-analysis have been used to study the modification of amino acids. Further, the thermal analysis of the protein has been studied with differential scanning calorimetry (DSC) and CD. Additionally, we have performed docking studies of H2O2 with Hb and Mb, which reveals that H2O2 molecules preferably attack the amino acids near heme group. We have also shown that N2 gas plasma has strong deformation action on biomolecules and compared to other gases plasma.

show abstract

“…There are some works that can be mentioned as examples of this situation. Juillard et al 146 used about 1000 times more buffer (bis-Tris) than ferric heme and apomyoglobin in their binding studies, whilst Seto et al 147 used 40 times more buffer than luciferin and EDTA; in this study, a sensitive bioluminescent enzyme immunoassay based on luciferin, where Mg(II) plays a vital role, was used. For BTP buffer, which is a strongly complexing ligand, some more examples are found in the literature.…”

Section: Cellular Biologymentioning

confidence: 99%

(Un)suitability of the use of pH buffers in biological, biochemical and environmental studies and their interaction with metal ions – a review

et al. 2015

View full text Add to dashboard Cite

The use of buffers to maintain the pH within a desired range is a very common practice in chemical, biochemical and biological studies.Among them, zwitterionic N-substituted aminosulfonic acids, usually known as Good'sbuffers, although widely used, can complex metals and interact with biological systems. The present work reviews, discusses and updates the metal complexation characteristics of thirty one commercially available buffers. In addition, their impact on biological systems is also presented. The influences of these buffers on the results obtained in biological, biochemical and environmental studies, with special focus on their interaction with metal ions, are highlighted and critically reviewed. Using chemical speciation simulations, based on the current knowledge of the metal-buffer stability constants, a proposal of the most adequate buffer to employ for a given metal ion is presented.

show abstract

Proton NMR study of myoglobin reconstituted with 3,7-diethyl-2,8-dimethyl iron porphyrin: Remarkable influence of peripheral substitution on heme rotation

Cited by 5 publications

References 27 publications

Dynamic Motion and Rearranged Molecular Shape of Heme in Myoglobin: Structural and Functional Consequences

Dynamic Motion and Rearranged Molecular Shape of Heme in Myoglobin: Structural and Functional Consequences

Influence of reactive species on the modification of biomolecules generated from the soft plasma

(Un)suitability of the use of pH buffers in biological, biochemical and environmental studies and their interaction with metal ions – a review

Contact Info

Product

Resources

About