Observation of the FeIVO stretching vibration of ferryl myoglobin by resonance Raman spectroscopy

Sitter, Andrew J.; Reczek, Catherine M.; Terner, James

doi:10.1016/0167-4838(85)90301-2

Cited by 105 publications

(90 citation statements)

References 44 publications

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“…In the linear Fe-C-N structure, the frequencies of the Fe-CN stretching ((Fe-C)) and ␦(FeCN) modes should exhibit a linear and a zigzag pattern, respectively, upon the isotope substitution in the order of 12 C 14 N, 13 C 14 N, 12 C 15 N, and 13 C 15 N. The (Fe-C) and ␦(FeCN) RR bands were first observed for metHb III isolated from Chironomus thummi thummi (metHb CTT III) at 453 and 412 cm Ϫ1 (33). The corresponding frequencies for human metHbA (34) and sperm whale metMb (35) are similar to those of metHb CTT III. For peroxidases, however, the order of (Fe-C) and ␦(FeCN) frequencies was reversed: (Fe-C) ϭ 361 and ␦(FeCN) ϭ 454 cm Ϫ1 for myeloperoxidase (36), (Fe-C) ϭ 360 and ␦(FeCN) ϭ 422 cm Ϫ1 for horseradish peroxidase (37), and (Fe-C) ϭ 360 and ␦(FeCN) ϭ 453 cm Ϫ1 for lactoperoxidase (38).…”

Section: Differences Between 430-and 455-nm Forms Of P450-isocyanidesupporting

confidence: 50%

Elucidation of the Differences between the 430- and 455-nm Absorbing Forms of P450-Isocyanide Adducts by Resonance Raman Spectroscopy

Tomita

Ogo

Egawa

et al. 2001

Journal of Biological Chemistry

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Cytochromes P450 (P450s) 1 belong to a superfamily of thiolate-coordinated heme proteins and are involved in the oxidative metabolism of various endogenous and exogenous organic compounds, catalyzing monooxygenase reactions. The x-ray crystallographic structures of five bacterial P450s currently available (1-5) suggest that the general features of a protein structure are essentially conserved in all P450s, although many specific sites vary within individual molecules (2-5). It is well known that alkyl and phenyl isocyanide adducts of ferrous P450 enzymes from several sources such as microsomes (6 -10), mitochondria (11), and also certain fungi (12) exhibit two Soret bands around 430 and 455 nm. The relative intensity of these two bands has been found to be sensitive to pH. The 455 nm band increases with increasing pH at the expense of the 430 nm band. These observations have been interpreted to mean that the ferrous isocyanide derivatives of P450s exist in two interconvertible forms, the 430-and 455-nm forms hereafter, which are in a pH-dependent equilibrium (6 -12).Studies of ferrous isocyanide derivatives of P450s, mostly of the hepatic microsomal P450s, have revealed several aspects of the 430-and 455-nm forms. For instance, the 430-nm form gives ␣ and ␤ bands around 560 and 530 nm, while the 455-nm form exhibits them around 580 and 555 nm (8, 9). It has also been found that the pK a with respect to the equilibrium between the 430-and 455-nm forms varies over P450 species (9, 12).The reality in the differences between the two interconvertible forms, however, remains elusive. This is partly due to the fact that ferrous isocyanide derivatives of many P450s undergo a gradual denaturation, particularly under acidic as well as alkaline conditions (6, 7). Therefore, observations on the derivatives have been successful in a pH range from 6 to 8 at which populations of the 430-and 455-nm forms in the equilibrium are in the same order of magnitude (6 -9). Such a limitation on the experimental conditions makes it difficult to investigate each of these interconvertible forms individually.Among P450 species so far studied, P450nor (CYP 55A1 in the systematic nomenclature system (13)) purified from denitrifying fungus Fusarium oxysporum (14) exhibits the spectral properties characteristic of P450 (14 -16) and belongs to the P450 superfamily (17). Nevertheless, this P450 has no monooxygenase activity. Instead P450nor catalyzes the reduction of NO to N 2 O by accepting electrons directly from NADH (14). Especially interesting is that P450nor has the highest pK a value for the equilibrium between the 430-and 455-nm forms of the ferrous isocyanide derivatives (12). Although the pK a value was not determined exactly, it has been observed that ethyl, n-butyl, and t-butyl isocyanide adducts of ferrous P450nor are essentially in the 430-nm form in pH ranges below 7.25 (12). Therefore, the ferrous isocyanide derivatives of P450nor are capable of being studied as the best representative of the 430-nm form.On the other hand, P450cam...

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Section: Differences Between 430-and 455-nm Forms Of P450-isocyanidesupporting

confidence: 50%

Elucidation of the Differences between the 430- and 455-nm Absorbing Forms of P450-Isocyanide Adducts by Resonance Raman Spectroscopy

Tomita

Ogo

Egawa

et al. 2001

Journal of Biological Chemistry

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“…3 shows low resolution (ϳ2 cm Ϫ1 resolved) Soret excitation at 413 nm rRaman spectra between 600 and 1600 cm Ϫ1 of resting ferric (lower trace) and hydrogen peroxide treated Mb (middle trace) at pH 6.8. The spectra show typical Raman shifts in accordance with full conversion of ferric Mb to Mb compound II (85,86) as seen by the shift of the oxidation state 4 heme core mode from 1369 -1370 to 1375 cm Ϫ1 and by the decrease of the ferric 2 heme core mode at 1563 cm Ϫ1 . Similar shifts (Fig.…”

Section: Formation Of Mb Compound II In Crystalsmentioning

confidence: 83%

Crystallographic and Spectroscopic Studies of Peroxide-derived Myoglobin Compound II and Occurrence of Protonated FeIV–O

Hersleth

Uchida

Røhr

et al. 2007

Journal of Biological Chemistry

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“…3 The ferryl species have been also reported using resonance Raman. To understand the effects of the HbI distal pocket on the ferryl intermediates, we discuss our findings in light of previous work done on Mb, 14 cytochrome c oxidase, [15][16][17] cytochrome bo, 18 and peroxidases. 14,19 These studies suggest a greater amount of coupling of the ferryl oxo internal coordinate with other out of plane motions.…”

mentioning

confidence: 93%

“…To understand the effects of the HbI distal pocket on the ferryl intermediates, we discuss our findings in light of previous work done on Mb, 14 cytochrome c oxidase, [15][16][17] cytochrome bo, 18 and peroxidases. 14,19 These studies suggest a greater amount of coupling of the ferryl oxo internal coordinate with other out of plane motions. 14 The structural factors that influence the ferryl oxo stretching frequencies are the heme pocket polarity, the electron donating and withdrawing character of the porphyrin, 18 steric hydrogen bonding interactions, and the trans ligand effects.…”

mentioning

confidence: 93%

“…14,19 These studies suggest a greater amount of coupling of the ferryl oxo internal coordinate with other out of plane motions. 14 The structural factors that influence the ferryl oxo stretching frequencies are the heme pocket polarity, the electron donating and withdrawing character of the porphyrin, 18 steric hydrogen bonding interactions, and the trans ligand effects. 20 We report the rate constant value for the peroxidative oxidation of L. pectinata oxy-HbI and the structure of a suggested nonhydrogen bonded compound II.…”

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confidence: 97%

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Evidence for nonhydrogen bonded compound II in cyclic reaction of hemoglobin I from Lucina pectinata with hydrogen peroxide

et al. 2002

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Studies that elucidate the behavior of the hemoglobins (Hbs) and myoglobins upon reaction with hydrogen peroxide are essential to the development of oxygen carrier substitutes. Stopped-flow kinetics and resonance Raman data show that the reaction between hydrogen peroxide and oxygenated and deoxygenated ferric Hb I (oxy- and deoxy-HbI) from Lucina pectinata produce compound I and compound II ferryl species. The rate constants ratio (k23/k41) between the formation of compound II from compound I (k23) and the oxidation of the ferrous HbI (k41, i.e., 25 M(-1) s(-1)) of 12 x 10(-4) M suggests that HbI has a peroxidative capacity for removing H2O2 from solution. Resonance Raman presents the formation of both, met-aquo-HbI and compound II ferryl species in the cyclic reaction of HbI with H2O2. The ferric HbI species is maintained by the presence of H2O2; it can produce HbI compound I, or it can be reduced to a deoxy-HbI derivative to form HbI compound II upon reaction with H2O2. The compound II ferryl vibration frequency appears at 805 and 769 cm(-1) for HbIFe(IV)=(16)O and HbIFe(IV)=(18)O species, respectively. This ferryl mode indicates the absence of hydrogen bonding between the carbonyl group of the distal Q64 and the HbIFe(IV)=O ferryl moiety. The observation suggests that both the trans-ligand effect and the polarizabilty of the HbI heme pocket are responsible for the observed ferryl oxo vibrational energy. The vibrational mode also suggests that the carbonyl group of the distal Q64 is oriented toward the iron of the heme group, increasing the distal pocket electron density.

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Observation of the FeIVO stretching vibration of ferryl myoglobin by resonance Raman spectroscopy

Cited by 105 publications

References 44 publications

Elucidation of the Differences between the 430- and 455-nm Absorbing Forms of P450-Isocyanide Adducts by Resonance Raman Spectroscopy

Elucidation of the Differences between the 430- and 455-nm Absorbing Forms of P450-Isocyanide Adducts by Resonance Raman Spectroscopy

Crystallographic and Spectroscopic Studies of Peroxide-derived Myoglobin Compound II and Occurrence of Protonated FeIV–O

Evidence for nonhydrogen bonded compound II in cyclic reaction of hemoglobin I from Lucina pectinata with hydrogen peroxide

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