Histidine residues of myoglobin studied by 1H nuclear magnetic resonance spectroscopy

Bradbury, J. H.; Deacon, Susan L. M.; Ridgway, Michael D.

doi:10.1039/c39790000997

Cited by 7 publications

(5 citation statements)

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“…Resonance 11 (Figure 16a) shows a large degree of broadening at low pH at 20 °C but not at 40 °C, which is similar to the broadening behavior of resonance 12 in CNMb. We propose that the two resonances in CNMb and COMb probably arise from the same proton and, hence, tentatively assign resonance 11 in COMb to His-24 H-2, rather than as previously to His-64 H-2 (Bradbury et al, 1979(Bradbury et al, ,1981. The argument for the previous assignment, viz., the similarity of pK values ( 4.5) between resonance 21 (Figure 15) assigned to His-64 H-4 and resonance 11, is not applicable because of lack of connectivity between resonances 11 and 21 in a COSY 2D NMR spectrum (P. E. Wright, private communication).…”

Section: Resultsmentioning

confidence: 62%

“…Resonances 15 and 18 are not observed in metMb and are assigned to His-36 and His-97 by matching pAfs of H-2 resonances. The upfield resonance 21 was previously assigned to the distal histidine-64 H-4 (Bradbury et al, 1979) on the basis of proximity to the large ring current of the porphyrin and will be discussed in the accompanying paper (Bradbury & Carver, 1984). Resonance 20 is observed as a singlet in a Carr-Purcell spectrum (not shown) and is tentatively assigned to His-24, while resonance 13 may be from His-82.…”

Section: Resultsmentioning

confidence: 83%

“…Subsequently, assignment was made of the resonances of seven surface histidines in sperm whale ferric metMb (Cohen et al, 1972;Hayes et al, 1975;. Ohms et al (1979) observed nine H-2 resonances that shifted with pH in oxyMb, and we observed the H-2 and H-4 resonances of the titrating histidines in COMb and oxyMb (Bradbury et al, 1979(Bradbury et al, , 1981; the proximal histidine residue (His-93) does not titrate. The aromatic region of the 13C 0006-2960/84/0423-4890$01.50/0 to deprotonation of His-97, pK -5.6) and another shift at pK = 10.8 ± 0.3.…”

Section: Most Of the Earlymentioning

confidence: 84%

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Assignment of proton NMR resonances of histidine and other aromatic residues in met-, cyano-, oxy-, and (carbon monoxy)myoglobins

Carver¹,

Bradbury²

1984

Biochemistry

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The resolved 1H NMR resonances of the aromatic region in the 270-MHz NMR spectrum of sperm whale, horse, and pig metmyoglobin (metMb) have been assigned, including the observable H-2 and H-4 histidine resonances, the tryptophan H-2 resonances, and upfield-shifted resonances from one tyrosine residue. The use of different Mb species, carboxymethylation, and matching of pK values allows the assignment of the H-4 resonances, which agree in only three cases out of seven with scalar-correlated two-dimensional NMR spectroscopy assignments by others. The conversion to hydroxymyoglobin at high pH involves rearrangements throughout the molecule and is observed by many assigned residues. In sperm whale ferric cyanomyoglobin, nine H-2 and eight H-4 histidine resonances have been assigned, including the His-97 H-2 resonance and tyrosine resonances from residues 103 and 146. The hyperfine-shifted resonances from heme and near-heme protons observe a shift with a pK = 5.3 +/- 0.3 (probably due to deprotonation of His-97, pK = 5.6) and another shift at pK = 10.8 +/- 0.3. The spectrum of high-spin ferrous sperm whale deoxymyoglobin is very similar to that of metMb, which allows the assignment of seven surface histidine H-2 and H-4 resonances and also resonances from the two tryptophan residues and one tyrosine. In diamagnetic sperm whale (carbon monoxy)myoglobin (COMb), 10 His H-2 and 11 His H-4 resonances are observed, and 8 H-2 and 9 H-4 resonances are assigned, including His-64 H-4, the distal histidine. This important resonance is not observed in sperm whale oxymyoglobin, which in general shows very similar titration curves to COMb. Histidine-36 shows unusual titration behavior in the paramagnetic derivatives but normal behavior in the diamagnetic derivatives, which is discussed in the accompanying paper [Bradbury, J. H., & Carver, J. A. (1984) Biochemistry (following paper in this issue)].

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Section: Resultsmentioning

confidence: 62%

Section: Resultsmentioning

confidence: 83%

Section: Most Of the Earlymentioning

confidence: 84%

See 1 more Smart Citation

Assignment of proton NMR resonances of histidine and other aromatic residues in met-, cyano-, oxy-, and (carbon monoxy)myoglobins

Carver¹,

Bradbury²

1984

Biochemistry

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“…For example, the 13C NMR studies of horse MbmCN indicate a pK value of 5.3 for either the proximal or the distal histidine (Wilbur & Allerhand, 1977) while 13CO NMR studies of sperm whale and horse MbnCO show an apparent pK between 5 and 6 for the 13CO NMR shifts (Moon et al, 1977). Proton NMR studies of sperm whale Mbn02 indicate distal histidine protonation with a pK of 5.7 (Ohms et al, 1979) while for MbnCO the value is reported to be 5.2 ± 0.2 (Bradbury et al, 1979). The results of temperaturejump measurements on sperm whale Mbm-imidazole (Goldsack et al, 1966) and absorption measurements on MbnCO (Hayashi et al, 1976) also suggest that the distal histidine hydrogen bonds to the sixth ligand with a pK of about 5.7.…”

Section: Resultsmentioning

confidence: 99%

Resonance Raman and absorption spectroscopic detection of distal histidine-fluoride interactions in human methemoglobin fluoride and sperm whale metmyoglobin fluoride: measurements of distal histidine ionization constants

Asher¹,

Adams²,

Schuster³

1981

Biochemistry

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The pH dependence of the resonance Raman and absorption spectra of human methemoglobin fluoride (HbIIIF) and sperm whale metmyoglobin fluoride (MbIIIF) has been examined. Both the Raman and absorption spectra of HbIIIF and MbIIIF indicate the existence at alkaline pH of an equilibrium between the hydroxide and fluoride complexes. The absorption maxima of HbIIIF and MbIIIF solutions shift to longer wavelengths as the pH is decreased from neutrality. The Raman data show a corresponding shift of the 461- and 468-cm-1 Fe-F vibrational stretching peaks at pH 7.0 [Asher, S. A., & Schuster, T. M. (1979) Biochemistry 18, 5377] to 399 and 407 cm-1 at acid pH in MbIIIF and HbIIIF, respectively. These shifts are interpreted to result from protonation of the distal histidine and the formation of a hydrogen bond to the fluoride ligand. Measurements of the pH dependence of the absorption and resonance Raman spectra give distal histidine ionization constants (apparent) corresponding to pK = 5.1 (+/- 0.1) for HbIIIF and pK = 5.5 (+/- 0.1) for MbIIIF. An examination of the distal histidine pK values and the frequency of the hydrogen-bonded Fe--F stretching vibration at pH 5.0 of HbIIIF with and without inositol hexaphosphate indicates little difference in the distal histidine--heme distance between the so-called R and T quaternary forms of HbIIIF. These results indicate that the changes in the electronic spectrum of HbIIIF that occur upon switching from the R to the T form do not result from alterations in (1) the iron--fluoride bond distance, (2) the iron out-of-heme plane distance, or (3) the distal histidine--fluoride distance.

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“…Until now, several analytical techniques have been developed for determination of PSA and Myo individually. These include chromatography [8,9], mass spectroscopy [10,11], fluorescence spectroscopy [12,13], nuclear magnetic resonance spectroscopy [14,15], white light reflectance spectroscopy [16,17], capillary electrophoresis [18], chemiluminescence [19], enzyme-linked immunosorbent assays (ELISA) [20,21], electrochemiluminescence [22,23], radioimmunoassay [24,25], time-resolved immunofluorometric assay [26], surface plasmon fluorescence immunoassay [27], bioluminescent immunoassay [28], electrochemical [29], surface-enhanced Raman scattering [24,30] and microcantilever method [31]. Of these methods, biosensors especially electrochemical types can offer some advantages in contrast to the commonly used sensing tools, including simultaneous analysis of biomarkers, capability of miniaturization, lower cost and simplicity of analysis [32][33][34].…”

Section: Introductionmentioning

confidence: 99%

Dual-modality impedimetric immunosensor for early detection of prostate-specific antigen and myoglobin markers based on antibody-molecularly imprinted polymer

Karami¹,

Bagheri

Johari-Ahar

et al. 2019

Talanta

120

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A new dual-modality immunosensor based on molecularly imprinted polymer (MIP) and a nanostructured biosensing layer has fabricated for the simultaneous detection of two important markers including prostatespecific antigen (PSA) and myoglobin (Myo) in human serum and urine samples. In the first step, 3,3′-dithiodipropionic acid di(N-hydroxysuccinimide ester) (DSP) was self-assembled on a gold screen printed electrode (SPE). Then, the target proteins were attached covalently to the DSP-SPE. The imprinted cocktail polymer ((MIP (PSA, Myo)-SPE)) was synthesized at the SPE surface using acrylamide as monomer, N,N′-methylenebisacrylamide as a crosslinker, and PSA and Myo as the templates, respectively. The MIP-SPE was specific for the impedimetric sensing of PSA and Myo. After that, a nanocomposite (NCP) was synthesized based on the decorated magnetite nanoparticles with multi-walled carbon nanotube, graphene oxide and specific antibody for PSA (Ab). Then, NCP incubated with (MIP(PSA, Myo)-SPE. The modified electrodes and synthesized nanoparticles were characterized using electrochemical impedance spectroscopy, dynamic light scattering, surface plasmon resonance and scanning electron microscopy. The limits of detections were found to be 5.4 pg mL −1 and 0.83 ng mL −1 with the linear dynamic ranges of 0.01-100 and 1-20000 ng mL −1 for PSA and Myo, respectively. The ability of proposed biosensor to detect PSA and Myo simultaneously with high sensitivity and specificity offers a powerful opportunity for the new generation of biosensors. This dual-analyte specific receptors-based device is highly desired for the integration with lab-on-chip kits to measure a wide panel of biomarkers present at ultralow levels during early stages of diseases progress.

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Histidine residues of myoglobin studied by 1H nuclear magnetic resonance spectroscopy

Cited by 7 publications

References 0 publications

Assignment of proton NMR resonances of histidine and other aromatic residues in met-, cyano-, oxy-, and (carbon monoxy)myoglobins

Assignment of proton NMR resonances of histidine and other aromatic residues in met-, cyano-, oxy-, and (carbon monoxy)myoglobins

Resonance Raman and absorption spectroscopic detection of distal histidine-fluoride interactions in human methemoglobin fluoride and sperm whale metmyoglobin fluoride: measurements of distal histidine ionization constants

Dual-modality impedimetric immunosensor for early detection of prostate-specific antigen and myoglobin markers based on antibody-molecularly imprinted polymer

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