Nitrosylhemoglobin wood. Effects of inositol hexaphosphate on thiol reactivity and electron paramagnetic resonance spectrum

Taketa, F.; Antholine, W E; Mauk, A. Grant; Libnoch, Joseph A.

doi:10.1021/bi00685a031

Cited by 39 publications

(9 citation statements)

References 21 publications

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“…IHP reduces the halftime of the reaction of 4,4/-dithiobispyridine with the sulfhydryl groups of deoxy-or CO-hemoglobin approximately twofold, but that with NO-hemoglobin 17-fold, indicative of a change in quaternary structure. Similar results have been obtained with nitrosylhemoglobin A by Taketa et al (1975). Adams and Schuster (1974) found that addition of IHP to human oxyhemoglobin in 0.1 M Hepes of pH 7.0 at 5.6°C produced changes in the visible absorption spectrum which they attributed to a change of quaternary structure to an "oxy T-form".…”

Section: Resultssupporting

confidence: 79%

Influence of globin structures on the state of the heme. IV. Ferrous low spin derivatives

Perutz¹,

Kilmartin²,

Nagai³

et al. 1976

Biochemistry

244

144

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Studies of high spin ferrous and ferric derivatives led us to conclude that in the quaternary R structure the state of the hemes is similar to that in the free alpha and beta subunits, but in the T structure a tension acts on the hemes which tries to pull the iron and the proximal histidine further from the plane of the porphyrin. We have now studied the effect of inositol hexaphosphate (IHP) on the three low spin ferrous compounds of hemoglobin with O2, CO, and NO. IHP failed to switch the quaternary structure of carbonmonoxy- and oxyhemoglobin A to the T state, but merely caused a transition to an as yet undefined modification of the R structure. IHP is known to cause a switch to the T structure in hemoglobin Kansas. We have found that this switch induces red shifts of the visible alpha and beta absorption bands and the appearance of a shoulder on the red side of the alpha band; these changes are very weak in carbonmonoxy- and slightly stronger in oxyhemoglobin Kansas. As already noted by previous authors, addition of IHP to nitrosylhemoglobin A induces all the changes in uv absorption and CD spectra, sulfhydryl reactivities, and exchangeable proton resonances normally associated with the R leads to T transition, and is accompanied by large changes in the Soret and visible absorption bands. Experiments with nitrosyl hybrids show that these changes in absorption are caused predominantly by the hemes in the alpha subunits. In the accompanying paper Maxwell and Caughey (J. C. Maxwell and W. S. Caughey (1976), Biochemistry, following paper in this issue) report that the NO in nitrosylhemoglobin without IHP gives a single ir stretching frequency characteristic for six-coordinated nitrosyl hemes; addition of IHP causes the appearance of a second ir band, of intensity equal to that of the first, which is characteristic for five-coordinated nitrosyl hemes. Taken together, these results show that the R leads to T transition causes either a rupture or at least a very dramatic stretching of the bond from the iron to the heme-linked histidine, such that an equilibrium is set up between five- and six-coordinated hemes, biased toward five-coordinated hemes in the alpha and six-coordinated ones in the beta subunits. The reason why IHP can switch nitrosyl-, but not carbonmonoxy- or oxyhemoglobin A, from the R to the T structure is to be found in the weakening of the iron-histidine bond by the unpaired NO electron and by the very short Fe-NO bond length.

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Section: Resultssupporting

confidence: 79%

Influence of globin structures on the state of the heme. IV. Ferrous low spin derivatives

Perutz¹,

Kilmartin²,

Nagai³

et al. 1976

Biochemistry

244

144

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“…Five-coordinate and six-coordinate ferrous-NO complexes with histidine as the proximal ligand have unique hyperfine and superhyperfine splitting patterns (24). Many five-coordinate and sixcoordinate ferrous-NO complexes of hemoproteins and model compounds have been reported (22,25,26). Five-coordinate ferrous heme-[ 14 N]NO complexes give a spectrum with three prominent lines which can be simplified to two prominent lines when [ 15 N]NO is used.…”

Section: Discussionmentioning

confidence: 99%

Structural Changes in the Heme Proximal Pocket Induced by Nitric Oxide Binding to Soluble Guanylate Cyclase

et al. 1998

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When expressed in Escherichia coli, the heme domain [beta1(1-385)] of rat lung soluble guanylate cyclase (sGC) is isolated with a stoichiometric amount of bound heme [Zhao, Y., and Marletta, M. A. (1997) Biochemistry 36, 15959-15964]. Nitric oxide (NO) binding to the heme in beta1(1-385) leads to cleavage of the Fe-His bond and formation of a five-coordinate NO-heme complex. Addition of imidazole to the five-coordinate NO complex shifts the Soret peak from 399 to 420 nm, which appears to result from the formation of a six-coordinate NO complex. Removal of the added imidazole by gel filtration results in formation of the five-coordinate NO complex once again. The EPR spectrum of the putative six-coordinate NO complex has nine distinct derivative-shaped lines (a triplet of triplets), which is the signature spectrum of a six-coordinate NO complex with two nitrogen atoms as the axial ligands. [15N]Imidazole simplifies the six-coordinate NO complex EPR spectrum to six distinct derivative-shaped lines (a triplet of doublets), indicating that the other axial ligand in the six-coordinate NO complex is an imidazole molecule. These results show that NO binding to sGC not only leads to the cleavage of the Fe-His bond but also induces a conformational change which opens the heme proximal pocket large enough to accommodate an exogenous imidazole molecule. These observations have important implications for determining the NO activation mechanism of sGC.

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“…It appears that these iron-ligand vibrations may be resonance enhanced via porphyrin -* transitions. Upon l^íitric oxide (NO) has been employed as a probe to detect the conformational change of the heme moiety in hemoglobin (Hb) when the quaternary structure is switched from the R to the T form (Rein et al, 1972;Cassoly, 1974;Taketa et al, 1975; Maxwell & Caughey, 1976;Perutz et al, 1976). Electron paramagnetic resonance (EPR) studies revealed that human nitrosylhemoglobin A (nitrosyl-HbA) in the R strucf From the School of Chemistry, Georgia Institute of Technology, Atlanta, Georgia 30332.…”

mentioning

confidence: 99%

Resonance Raman investigation of nitric oxide bonding in nitrosylhemoglobin A and -myoglobin: detection of bound nitrogen-oxygen stretching and iron-nitric oxide stretching vibrations from the hexacoordinated nitric oxide-heme complex

Tsubaki¹,

Yu²

1982

Biochemistry

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With excitation at 406.7 nm, we have observed the resonance Raman enhancement of the bound v(N-O) stretch at approximately 1623 cm-1 in nitrosylhemoglobin A and nitrosylmyoglobin, indicating the existence of a charge-transfer transition underlying the strong Soret band. The v(Fe-NO) stretch at 551 cm-1 has also been detected in the Soret as well as in the Q-band region, a phenomenon similar to the v(Fe-O2) and v(Fe-CO) stretches in oxy and carbon monoxy hemoproteins. It appears that these iron-ligand vibrations ay be resonance enhanced via porphyrin pi leads to pi transitions. Upon addition of inositol hexaphosphate at pH 6.0, the v(Fe-NO) stretch at 551 cm-1 and a low-frequency mode at 301 cm-1 exhibit an intensity decrease by approximately one-half. Contrary to the work of Stong et al. [Stong, J. D., Burke, J. M., Daly, P., Wright. P., & Spiro, T. G. (1980) J. Am. Chem. Soc. 102, 5815], who employed an excitation wavelength at 454.5 nm, we observed no intensity increase at 592 cm-1 attributable to the v(Fe-NO) stretch from the pentacoordinated NO-heme complex in the alpha subunits.

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Nitrosylhemoglobin wood. Effects of inositol hexaphosphate on thiol reactivity and electron paramagnetic resonance spectrum

Cited by 39 publications

References 21 publications

Influence of globin structures on the state of the heme. IV. Ferrous low spin derivatives

Influence of globin structures on the state of the heme. IV. Ferrous low spin derivatives

Structural Changes in the Heme Proximal Pocket Induced by Nitric Oxide Binding to Soluble Guanylate Cyclase

Resonance Raman investigation of nitric oxide bonding in nitrosylhemoglobin A and -myoglobin: detection of bound nitrogen-oxygen stretching and iron-nitric oxide stretching vibrations from the hexacoordinated nitric oxide-heme complex

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