Resonance Raman studies of methemoglobin derivatives at room temperature and 77 K

Cho, K.C.; Remba, R.D.; Fitchen, D. B.

doi:10.1016/0005-2795(81)90162-8

Cited by 10 publications

(14 citation statements)

References 13 publications

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“…It is noted that these rR data are in good agreement with previous rR studies on isolated Hb protein. 1 , 5 , 12 …”

Section: Resultsmentioning

confidence: 99%

“…Resonance Raman (rR) spectroscopy is a powerful technique for the characterization of the heme–CN – adducts, allowing the detection and monitoring of all possible vibrations associated with the Fe–C≡N fragment, including the ν(Fe–CN) stretching, δ(Fe–CN) bending, and ν(C≡N) stretching modes; 12 , 14 , 15 , 18 − 20 for example, the rR studies of isolated HbCN protein were previously published. 1 , 5 , 12 …”

Section: Introductionmentioning

confidence: 99%

“…Resonance Raman (rR) spectroscopy is a powerful technique for the characterization of the heme− CN − adducts, allowing the detection and monitoring of all possible vibrations associated with the Fe−CN fragment, including the ν(Fe−CN) stretching, δ(Fe−CN) bending, and ν(CN) stretching modes; 12,14,15,18−20 for example, the rR studies of isolated HbCN protein were previously published. 1,5,12 The enhancement of specific vibrational modes, their frequencies, and patterns of isotopic shifts permit a clear distinction between the linear, tilted, and bent configurations of the Fe−CN fragment. The linear geometry of the Fe− CN linkage naturally abolishes the activation of the δ(Fe− CN) bending mode.…”

Section: ■ Introductionmentioning

confidence: 99%

“…It is noted that these rR data are in good agreement with previous rR studies on isolated Hb protein. 1,5,12 Figure 3 shows the rR spectra in the low-frequency region of the HbCN sample inside RBCs, its 13 CN, C 15 N, and 13 C 15 N isotopic analogues, and the CN− 13 CN, CN−C 15 N, and CN− 13 C 15 N difference traces (Panel A). The rR spectra are normalized to the dominant ν 7 mode located at 678 cm −1 .…”

Section: ■ Introductionmentioning

confidence: 99%

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Probing Heme Active Sites of Hemoglobin in Functional Red Blood Cells Using Resonance Raman Spectroscopy

et al. 2021

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The UV–vis absorption, Raman imaging, and resonance Raman (rR) spectroscopy methods were employed to study cyanohemoglobin (HbCN) adducts inside living functional red blood cells (RBCs). The cyanide ligands are especially optically sensitive probes of the active site environment of heme proteins. The rR studies of HbCN and its isotopic analogues ( 13 CN – , C 15 N – , and 13 C 15 N – ), as well as a careful deconvolution of spectral data, revealed that the ν(Fe–CN) stretching, δ(Fe–CN) bending, and ν(C≡N) stretching modes occur at 454, 382, and 2123 cm –1 , respectively. Interestingly, while the ν(Fe–CN) modes exhibit the same frequencies in both the isolated and RBC-enclosed hemoglobin molecules, small frequency differences are observed in the δ(Fe–CN) bending modes and the values of their isotopic shifts. These studies show that even though the overall tilted conformation of the Fe–C≡N fragment in the isolated HbCN is preserved in the HbCN enclosed within living cells, there is a small difference in the degree of distortion of the Fe–C≡N fragment. The slight changes in the ligand geometry can be reasonably attributed to the high ordering and tight packing of Hb molecules inside RBCs.

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“…It is noted that these rR data are in good agreement with previous rR studies on isolated Hb protein. 1 , 5 , 12 …”

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: ■ Introductionmentioning

confidence: 99%

Section: ■ Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Probing Heme Active Sites of Hemoglobin in Functional Red Blood Cells Using Resonance Raman Spectroscopy

et al. 2021

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show abstract

“…4A (a) (65)(66)(67). A second set of marker bands is located at 3 ϭ 1476 cm Ϫ1 and 2 ϭ 1558 cm Ϫ1 , which likely stems from a small fraction of a high spin ferric form (68,69).…”

Section: Spectral Characterization Of Glb-33 Gd and A Suum Fmrf Gdmentioning

confidence: 99%

A Globin Domain in a Neuronal Transmembrane Receptor of Caenorhabditis elegans and Ascaris suum

Tilleman

Germani

Henau

et al. 2015

Journal of Biological Chemistry

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Heme-heme oxygenase complex. Structure of the catalytic site and its implication for oxygen activation.

Takahashi

Wang

Rousseau

et al. 1994

Journal of Biological Chemistry

120

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Resonance Raman studies of methemoglobin derivatives at room temperature and 77 K

Cited by 10 publications

References 13 publications

Probing Heme Active Sites of Hemoglobin in Functional Red Blood Cells Using Resonance Raman Spectroscopy

Probing Heme Active Sites of Hemoglobin in Functional Red Blood Cells Using Resonance Raman Spectroscopy

A Globin Domain in a Neuronal Transmembrane Receptor of Caenorhabditis elegans and Ascaris suum

Heme-heme oxygenase complex. Structure of the catalytic site and its implication for oxygen activation.

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