Resonance Raman investigation of myoglobin and hemoglobin

Bangcharoenpaurpong, O.; Schomacker, Kevin T.; Champion, P. M.

doi:10.1021/ja00331a045

Cited by 145 publications

(142 citation statements)

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“…This band gains resonance enhancement through B-excitation of such hemes, which typically maximizes near 435 nm [55,56]. Consistent with this assignment, the 229 cm −1 band is absent from the 413.1-nm spectra in Fig.…”

Section: The Heme Environment Of Fe(ii) Rhed Is Ph Sensitivesupporting

confidence: 73%

CO and NO bind to Fe(II) DiGeorge critical region 8 heme but do not restore primary microRNA processing activity

et al. 2016

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Section: The Heme Environment Of Fe(ii) Rhed Is Ph Sensitivesupporting

confidence: 73%

CO and NO bind to Fe(II) DiGeorge critical region 8 heme but do not restore primary microRNA processing activity

et al. 2016

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“…The analysis is performed on a Microway I860 add-on board for IBM-PC, using a Marquardt-type nonlinear least squares algorithm (24). The fitting parameters are M, ⌫, S i , , o , Q 0 ͌ b, and ␦ ͌ b; the values relative to high frequency modes are taken from resonance Raman spectra of human deoxyhemoglobin reported in the literature (25). As in previous work (14), we assume that the mutations investigated do not alter the frequency of these modes; this assumption is supported by the excellent quality of the fittings obtained (see Fig.…”

Section: Methodsmentioning

confidence: 71%

Modification of α-Chain or β-Chain Heme Pocket Polarity by Val(E11) → Thr Substitution Has Different Effects on the Steric, Dynamic, and Functional Properties of Human Recombinant Hemoglobin

Cupane

Leone

Militello

et al. 1997

Journal of Biological Chemistry

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The dynamic and functional properties of mutant deoxyhemoglobins in which either the ␤-globin Val 67 (E11) or the ␣-globin Val 62 (E11) is replaced by threonine have been investigated through the thermal evolution of the Soret absorption band in the temperature range 300 to 20 K and through the kinetics of CO rebinding after flash photolysis at room temperature. The conformational properties of the modified ␣ chain and ␤ chain distal heme pockets were also studied through x-ray crystallography and molecular modeling. The data obtained with the various techniques consistently indicate that the polar isosteric mutation in the distal side of the ␣ chain heme pocket has a larger effect on the investigated properties than the analogous mutation on the ␤ chain. We attribute the observed differences to the presence of a water molecule in the distal heme pocket of the modified ␣ chains, interacting with the hydroxyl of the threonine side chain. This is indicated by molecular modeling which showed that the water molecule present in the ␣ chain distal heme pocket can bridge by H bonding between Thr 62 (E11) and His 58 (E7) without introducing any unfavorable steric interactions. Consistent with the dynamic and functional data, the presence of a water molecule in the distal heme pocket of the modified ␤ chains is not observed by x-ray crystallography.

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“…16. The vibrational modes that couple to the electronic transition were taken from resonance Raman data (22,23), as described in ref. 16 for MbCO and in ref.…”

Section: Methodsmentioning

confidence: 99%

Structural factors controlling ligand binding to myoglobin: A kinetic hole-burning study

Ormos

Száraz

Cupane

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

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Using temperature-derivative spectroscopy in the temperature range below 100 K, we have studied the dependence of the Soret band on the recombination barrier in sperm whale carbonmonoxy myoglobin (MbCO) after photodissociation at 12 K. The spectra were separated into contributions from the photodissociated species, Mb*CO, and CObound myoglobin. The line shapes of the Soret bands of both photolyzed and liganded myoglobin were analyzed with a model that takes into account the homogeneous bandwidth, coupling of the electronic transition to vibrational modes, and static conformational heterogeneity. The analysis yields correlations between the activation enthalpy for rebinding and the model parameters that characterize the homogeneous subensembles within the conformationally heterogeneous ensemble. Such couplings between spectral and functional parameters arise when they both originate from a common structural coordinate. This effect is frequently denoted as ''kinetic hole burning.'' The study of these correlations gives direct insights into the structure-function relationship in proteins. On the basis of earlier work that assigned spectral parameters to geometric properties of the heme, the connections with the heme geometry are discussed. We show that two separate structural coordinates inf luence the Soret line shape, but only one of the two is coupled to the enthalpy barrier for rebinding. We give evidence that this coordinate, contrary to widespread belief, is not the iron displacement from the mean heme plane.

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Resonance Raman investigation of myoglobin and hemoglobin

Cited by 145 publications

References 0 publications

CO and NO bind to Fe(II) DiGeorge critical region 8 heme but do not restore primary microRNA processing activity

CO and NO bind to Fe(II) DiGeorge critical region 8 heme but do not restore primary microRNA processing activity

Modification of α-Chain or β-Chain Heme Pocket Polarity by Val(E11) → Thr Substitution Has Different Effects on the Steric, Dynamic, and Functional Properties of Human Recombinant Hemoglobin

Structural factors controlling ligand binding to myoglobin: A kinetic hole-burning study

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