NMR titration curves of histidine ring protons. 11. Near-heme histidine residues of deoxy- and oxymyoglobins

Ohms, J.; Hagenmaier, Hanspaul; Hayes, Melvin B.; Cohen, Jack S.

doi:10.1021/bi00575a034

Cited by 14 publications

(8 citation statements)

References 17 publications

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“…In both cases there are seven H-2 histidine resonances, and the titration curves are very similar, hence allowing assignments based on metMb. The results of Ohms et al (1979) for sperm whale deoxyMb are generally in agreement with those presented here (Table VI), although they assigned an extra upfield resonance to His-97 H-2, which we have assigned to His-81 H-4 (see Tables II and IV).…”

Section: Resultssupporting

confidence: 90%

“…A Carr-Purcell spectrum (not shown) shows that resonance 9 is a "Tentative assignment, see text. 6Results of Ohms et al (1979). Their resonance tabulated here as belonging to His-97 was tentatively assigned by them to His-64.…”

Section: Resultsmentioning

confidence: 88%

“…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%

“…and are defined in Table I. 4Results of Ohms et al (1979). " Definitions of and are given in Table I.…”

Section: Resultsmentioning

confidence: 99%

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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: Resultssupporting

confidence: 90%

Section: Resultsmentioning

confidence: 88%

Section: Most Of the Earlymentioning

confidence: 84%

“…and are defined in Table I. 4Results of Ohms et al (1979). " Definitions of and are given in Table I.…”

Section: Resultsmentioning

confidence: 99%

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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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“…Histidine protons had not been studied in equine ferric cyanomyoglobin, although they have been assigned in the closely homologous sperm whale ferric cyanomyoglobin ). His protons have been observed and assigned in many species and forms of myoglobin in extensive studies by independent groups (Bothelho & Gurd, 1978a,b;Ohms et al, 1979;. Myoglobins possess a large number of His residues; many of these are in environments where there is sufficient conformational flexibility to give rise to sharp singlets for the nonexchangeable C2 and C4 protons.…”

Section: Mbfejiicnmentioning

confidence: 99%

Proton NMR spectroscopy of sulfmyoglobin

Timkovich¹,

Vavra²

1985

Biochemistry

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The 1H NMR spectra of ferrous sulfmyoglobin, metsulfmyoglobin, and ferric cyanosulfmyoglobin were obtained at 300 MHz. Hyperfine-shifted resonances are observed in the case of metsulfmyoglobin and ferric cyanosulfmyoglobin that have line widths and cover a chemical shift range that are comparable to the corresponding forms of normal myoglobin. Two methyl resonances are observed in the spectrum of ferric cyanosulfmyoglobin at 44.19 and 25.48 ppm (25 degrees C, pH 8.3) that have been assigned to heme methyls at the 8- and 5-positions on the basis of pH titration effects homologous to the corresponding methyl resonances in ferric cyanomyoglobin. Examination of aromatic region resonances and the pH titration profiles of histidine resonances lead to the conclusion that the overall conformation of sulfmyoglobin was highly homologous to that of normal myoglobin and afforded assignments of histidine residues of the former. The most likely position for the addition of a sulfur atom to the heme of sulfmyoglobin is pyrrole ring A, with ring B a possible, but less likely, alternative.

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Dependence of Axial Ligand Force Constants upon Globin Structure in Hemoglobin and Myoglobin

Asher¹,

Schuster²

1982

Hemoglobin and Oxygen Binding

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NMR titration curves of histidine ring protons. 11. Near-heme histidine residues of deoxy- and oxymyoglobins

Cited by 14 publications

References 17 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

Proton NMR spectroscopy of sulfmyoglobin

Dependence of Axial Ligand Force Constants upon Globin Structure in Hemoglobin and Myoglobin

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