Two types of conformers with distinct Fe-C-O configuration in the ferrous CO complex of horseradish peroxidase. Resonance Raman and infarared spectroscopic studies with native and deuteroheme-substituted enzymes.

Uno, Tadayuki; Nishimura, Yuki; Tsuboi, Masamichi; Makino, Ryu; Iizuka, Tetsutarō; Ishimura, Yuzuru

doi:10.1016/s0021-9258(18)61227-x

Cited by 112 publications

(110 citation statements)

References 42 publications

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“…5 B. The absorption maximum at 290 K is at 1911 cm Ϫ1 , which is in agreement with a previous study (Uno et al, 1987). The peak narrows from 9 to 6 cm Ϫ1 , full width at half maximum, in going from 290 to 20 K. A peak seen at 1903 cm Ϫ1 has the same position and temperature dependence as the substrate-free protein (Fig.…”

Section: Temperature Dependence Of the Co Ir Absorption Band Of Hrp(co)supporting

confidence: 91%

“…This value Parameters for HRP(CO) and HRP(CO)-BHA are respectively A 1 ϭ 0.7 ⅐ 10 4 and 2.6 ⅐ 10 4 cm Ϫ2 ; B 1 ϭ 1.4 ⅐ 10 6 and 0.7 ⅐ 10 6 cm Ϫ3 ; and h ϭ 150 cm Ϫ1 . reproduces the value within 1 cm Ϫ1 observed by previous workers for the enzyme in aqueous solution (Barlow et al, 1976;Smulevich et al, 1986;Uno et al, 1987). The protein, purified as described in Methods, shows a single IR absorption band within the resolution of the spectrum.…”

Section: Temperature Dependence Of the Co Ir Absorption Band Of Hrp(co)supporting

confidence: 87%

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Influence of Static and Dynamic Disorder on the Visible and Infrared Absorption Spectra of Carbonmonoxy Horseradish Peroxidase

Kaposi

Vanderkooi

Wright

et al. 2001

Biophysical Journal

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Spectroscopy of horseradish peroxidase with and without the substrate analog, benzohydroxamic acid, was monitored in a glycerol/water solvent as a function of temperature. It was determined from the water infrared (IR) absorption that the solvent has a glass transition at 170-180 K. In the absence of substrate, both the heme optical Q(0,0) absorption band and the IR absorption band of CO bound to heme broaden markedly upon heating from 10-300 K. The Q(0,0) band broadens smoothly in the whole temperature interval, whereas the IR bandwidth is constant in the glassy matrix and increases from 7 to 16 cm(-1) upon heating above the glass transition. Binding of substrate strongly diminishes temperature broadening of both the bands. The results are consistent with the view that the substrate strongly reduces the amplitude of motions of amino acids forming the heme pocket. The main contribution to the Q(0,0) bandwidth arises from the heme vibrations that are not affected by the phase transition. The CO band thermal broadening stems from the anharmonic coupling with motions of the heme environment, which, in the glassy state, are frozen in. Unusually strong temperature broadening of the CO band is interpreted to be caused by thermal population of a very flexible excited conformational substrate. Analysis of literature data on the thermal broadening of the A(0) band of Mb(CO) (Ansari et al., 1987. Biophys. Chem. 26:337-355) shows that such a state presents itself also in myoglobin.

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Section: Temperature Dependence Of the Co Ir Absorption Band Of Hrp(co)supporting

confidence: 91%

Section: Temperature Dependence Of the Co Ir Absorption Band Of Hrp(co)supporting

confidence: 87%

Influence of Static and Dynamic Disorder on the Visible and Infrared Absorption Spectra of Carbonmonoxy Horseradish Peroxidase

Kaposi

Vanderkooi

Wright

et al. 2001

Biophysical Journal

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“…We plot the correlation between the Fe-CO and CO stretching frequencies together with data for other heme proteins in Figure . The points for IsdG and IsdI are on the line formed by heme proteins having histidine as the axial ligand. − These results further corroborate that the axial ligand is the neutral form of histidine.…”

Section: Resultssupporting

confidence: 52%

Unique Electronic Structures of the Highly Ruffled Hemes in Heme-Degrading Enzymes of Staphylococcus aureus, IsdG and IsdI, by Resonance Raman and Electron Paramagnetic Resonance Spectroscopies

et al. 2020

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Staphylococcus aureus uses IsdG and IsdI to convert heme into a mixture of staphylobilin isomers, 15-oxo-β-bilirubin and 5-oxo-δ-bilirubin, formaldehyde, and iron. The highly ruffled heme found in the heme-IsdI and IsdG complexes has been proposed to be responsible for the unique heme degradation products. We employed resonance Raman (RR) and electron paramagnetic resonance (EPR) spectroscopies to examine the coordination and electronic structures of heme bound to IsdG and IsdI. Heme complexed to IsdG and IsdI is coordinated by a neutral histidine. The trans ligand is hydroxide in the ferric alkaline form of both proteins. In the ferric neutral form at pH 6.0, heme is six-coordinated with water as the sixth ligand for IsdG and is in the mixture of the five-coordinated and six-coordinated species for IsdI. In the ferrous CO-bound form, CO is strongly hydrogen bonded with a distal residue. The marker lines, ν2 and ν3, appear at frequencies that are distinct from other proteins having planar hemes. The EPR spectra for the ferric hydroxide and cyanide states might be explained by assuming the thermal mixing of the d-electron configurations, (d xy )2(d xz ,d yz )3 and (d xz ,d yz )4(d xy )1. The fraction for the latter becomes larger for the ferric cyanide form. In the ferric neutral state at pH 6.0, the quantum mechanical mixing of the high and intermediate spin configurations might explain the peculiar frequencies of ν2 and ν3 in the RR spectra. The heme ruffling imposed by IsdG and IsdI gives rise to unique electronic structures of heme, which are expected to modulate the first and subsequent steps of the heme oxygenation.

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“…This property has been exploited using the CO frequency (n CO ) as a vibrational probe in heme protein's active sites. 98,99 Several works 100,101 noted a negative correlation between n FeÀCO and n CO . Provided that the sixth ligand is unchanged, these two frequencies have been found to correlate linearly.…”

Section: The Heme-co Complexmentioning

confidence: 99%

Modeling heme proteins using atomistic simulations

Bikiel

Boechi

Capece

et al. 2006

Phys. Chem. Chem. Phys.

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Heme proteins are found in all living organisms, and perform a wide variety of tasks ranging from electron transport, to the oxidation of organic compounds, to the sensing and transport of small molecules. In this work we review the application of classical and quantum-mechanical atomistic simulation tools to the investigation of several relevant issues in heme proteins chemistry: (i) conformational analysis, ligand migration, and solvation effects studied using classical molecular dynamics simulations; (ii) electronic structure and spin state energetics of the active sites explored using quantum-mechanics (QM) methods; (iii) the interaction of heme proteins with small ligands studied through hybrid quantum mechanics-molecular mechanics (QM-MM) techniques; (iv) and finally chemical reactivity and catalysis tackled by a combination of quantum and classical tools.

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Two types of conformers with distinct Fe-C-O configuration in the ferrous CO complex of horseradish peroxidase. Resonance Raman and infarared spectroscopic studies with native and deuteroheme-substituted enzymes.

Cited by 112 publications

References 42 publications

Influence of Static and Dynamic Disorder on the Visible and Infrared Absorption Spectra of Carbonmonoxy Horseradish Peroxidase

Influence of Static and Dynamic Disorder on the Visible and Infrared Absorption Spectra of Carbonmonoxy Horseradish Peroxidase

Unique Electronic Structures of the Highly Ruffled Hemes in Heme-Degrading Enzymes of Staphylococcus aureus, IsdG and IsdI, by Resonance Raman and Electron Paramagnetic Resonance Spectroscopies

Modeling heme proteins using atomistic simulations

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