Low-frequency vibrations in resonance Raman spectra of horse heart myoglobin. Iron-ligand and iron-nitrogen vibrational modes

Desbois, Alain; Lutz, Marc; Banerjee, R.

doi:10.1021/bi00575a019

Cited by 113 publications

(98 citation statements)

References 41 publications

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“…The 220 cm -1 band must thus correspond to an out-of-plane vibrational mode. This is in accord with its assignment as an Fe-Ne(proximal histidine) stretch [11,[15][16][17] but not as an Fe-N(pyrrole) vibration [14]. The Fe-Ne(proximal histidine) stretching band occurs at 219-221 cm -1 for deoxymyoglobin and 221-222 cm -1 for deoxy-leghemoglobin ( fig.2,3), i.e., there is no significant difference in bond strength.…”

Section: Methodssupporting

confidence: 82%

“…No other bands are sensitive to the isotopic substitution. Fe-O: stretching frequencies have also been measured for a series of hemoglobins [11,12] and myoglobins [13,14]. The Fe-O: stretching band was observed at 567-572 cm -~ in oxy-hemoglobins while values of 572 cm -~ and 577 cm -~ have been reported for oxy-myoglobin.…”

Section: Methodsmentioning

confidence: 94%

“…Our work provides further support for this assignment. With irradiation at 457.9 nm (and also 441.6 nm [14]) all bands in the low wavenumber region show appreciable resonance enhancement ( fig.2). However, with excitation at 413.1 nm there is a general decrease in intensity of the Raman bands relative to that at 220 cm -1 ( fig.3).…”

Section: Methodsmentioning

confidence: 98%

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Resonance Raman studies of soybean leghemoglobin and myoglobin

1981

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Section: Methodssupporting

confidence: 82%

Section: Methodsmentioning

confidence: 94%

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Resonance Raman studies of soybean leghemoglobin and myoglobin

1981

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“…Indeed, if the Co-N-0 bond angle is < 180" there is a certain mixing between stretching and bending modes. Interestingly, this isotope-sensitive line at 573 cm-' is identical to the Fe-02 stretching frequency in oxy sperm whale myoglobin [3] and is very close to 567 cm-' found and assigned originally by Brunner in Hb A [2].…”

Section: Assignment Of Co-no Stretching Mode In Cobalt Hemoglobinssupporting

confidence: 84%

The cobalt‐nitrosyl stretching vibration as a sensitive resonance Raman probe for distal histidine‐nitrosyl interaction in monomeric hemoglobins

Thompson

Mizukami

et al. 1986

European Journal of Biochemistry

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The Co-NO stretching vibration has been assigned in the resonance Raman spectra of various cobaltMonomeric hemoglobins with a distal histidine (sperm whale myoglobin and leghemoglobin) exhibit this vibration at 573 -575 cm-', whereas hemoglobins without distal histidine (elephant myoglobin and insect hemoglobin from Chironomus thummi thummi, CTT 111) show this vibration in the range of 553 -558 cm-'. The Fe-NO stretching vibration which occurs in the range of 554-556 cm-' does not reflect the distal histidine-ligand interaction. Therefore, the Co-NO moiety which is isoelectronic with the Fe-02 moiety is a good monitor for distal effects on the exogenous ligand of hemoglobins, especially due to the fact that in hemoglobins with distal histidine the Fe-02 stretching vibration (567-572 cm-') is similar to the Co-NO stretching vibration.substituted monomeric hemoglobins by employing isotope-labeling of nitrosyl (14N160, 15N160 , 14~180).Cobalt-substituted hemes are capable of binding nitric oxide in the presence of nitrogen bases [l]. The cobalt-nitrosyl moiety is isoelectronic with the iron-dioxygen moiety. It is demonstrated in t h s paper that cobalt-substituted hemoglobins also bind nitric oxide. Therefore, the nitrosylated cobalt hemoglobins are of particular interest for investigating the interactions of the exogenous ligand with the protein side groups on the distal side of the heme. Since the Fe-02 stretching vibration has been first observed by Brunner in oxy Hb A [2] and later by other authors in many hemoglobins [3-61, it is of particular interest to find the corresponding Co-NO stretching frequency. The assignment of the CO-NO stretching mode is easier than that of the v(Fe-02) as various isotopically labelled nitric oxides (14N'60,'5N'60, 14N'80) are available. By comparison of the stretching vibrations of the Co-NO and Fe-02 bonds we can determine the similarities or differences between the metal-ligand bonding interactions in these isoelectronic systems.Four cobalt-substituted monomeric hemoglobins were studied via resonance Raman spectroscopy: sperm whale myoglobin, leghemoglobin from soybean, insect hemoglobin from Chironomus thummi thummi (CTT 111) and elephant myoglobin. These hemoglobins contain the same protoheme-IX as prosthetic groups but they are different with regard to their heme pockets. Thus, we expect that the pophyrin-protein or ligand-protein interactions are different in these hemoglobins. Sperm whale myoglobin has a distal histidine [7], whereas in elephant myoglobin this histidine is replaced by glutamine [S, 91. In CTT 111, the 'distal' hstidine is turned to the surface of the molecule and is thus incapable of interacting MATERIALS AND METHODSSperm whale myoglobin was purchased from Sigma Chemicals (St Louis, MO) and further purified as already described [ 131. Elephant myoglobin [S], leghemoglobin from soybean [14], and CTT 111 from Chironomus thummi thummi [15,16] were purified as described elsewhere. The preparation of cobaltous protoporphyrin-IX and the reconstitution of hemo...

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“…Thr-66 is in close proximity to the heme propionate in the crystal structure (12), which is consistent with the view that the hydrogen-bonding network including the heme propionates are perturbed by the mutation. In addition to the heme peripheral vibrations, the Fe-OH stretching mode ( Fe-OH ) can be observed in the low frequency region around 450ϳ560 cm Ϫ1 (37,38), and should be down-shifted by ϳ25 cm Ϫ1 upon the isotope substitution of 16 OH to 18 OH in the hydroxide bound ferric heme (37). The Fig.…”

mentioning

confidence: 99%

On the Relationship of Coral Allene Oxide Synthase to Catalase

Tosha

Uchida

Brash

et al. 2006

Journal of Biological Chemistry

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A heme domain of coral allene oxide synthase (cAOS) catalyzes the formation of allene oxide from fatty acid hydroperoxide. Although cAOS has a similar heme active site to that of catalase, cAOS is completely lacking in catalase activity. A close look at the hydrogen-bonding possibilities around the distal His in cAOS suggested that the imidazole ring is rotated by 180°relative to that of catalase because of the hydrogen bond between Thr-66 and the distal His-67. This could contribute to the functional differences between cAOS and catalase, and to examine this possibility, we mutated Thr-66 in cAOS to Val, the corresponding residue in catalase. In contrast to the complete absence of catalase activity in wild type (WT) cAOS, T66V had a modest catalase activity. On the other hand, the mutation suppressed the native enzymatic activity of the formation of allene oxide to 14% of that of WT cAOS. In the resonance Raman spectrum, whereas WT cAOS has only a 6-coordinate/high spin heme, T66V has a 5-coordinate/high spin heme as a minor species. Because catalase adopts a 5-coordinate/high spin structure, probably the 5-coordinate/high spin portion of T66V showed the catalase activity. Furthermore, in accord with the fact that the CN affinity of catalase is higher than that of WT cAOS, the CN affinity of T66V was 8-fold higher than that of WT cAOS, indicating that the mutation could mimic the heme active site in catalase. We, therefore, propose that the hydrogen bond between Thr-66 and distal His-67 could modulate the orientation of distal His, thereby regulating the enzymatic activity in cAOS.Allene oxides formed by the enzymatic dehydration of fatty acid hydroperoxides, the lipoxygenase (LOX) 4 products of polyunsaturated fatty acids, are involved in biosynthetic pathways of plants and invertebrates. The main plant pathway leads to jasmonic acid, which seems to be a physiological signaling molecule for several wound-and pathogeninduced responses (1). The conversion from fatty acid hydroperoxide to allene oxide in plants is catalyzed by a heme containing enzyme called allene oxide synthase (AOS) (2, 3). Plant AOS belongs to a subfamily of the fatty acid hydroperoxide metabolizing cytochrome P450s (P450s) designated as CYP74A (4 -6). Despite significant sequence homology of plant AOS to those of other P450s, the reaction of plant AOS is different from those of typical P450s (7,8). Plant AOS does not require the reductants and oxygen, and carries out the homolytic cleavage of the O-O bond in hydroperoxide, although typical P450s utilize two electrons and molecular oxygen for the hydroxylation of its substrate. Koljak et al. (1997) discovered and isolated a cDNA encoding a fusion protein of 8R-LOX and AOS from the Caribbean sea soft coral, Plexaura homomalla (9), the first example of an AOS found in animals. The fusion protein consists of a C-terminal 8R-LOX domain (79 kDa) and N-terminal heme-containing AOS domain (43 kDa). As shown in Scheme 1, reaction (i), the 8R-LOX domain initially catalyzes the oxygenation of arachidon...

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Low-frequency vibrations in resonance Raman spectra of horse heart myoglobin. Iron-ligand and iron-nitrogen vibrational modes

Cited by 113 publications

References 41 publications

Resonance Raman studies of soybean leghemoglobin and myoglobin

Resonance Raman studies of soybean leghemoglobin and myoglobin

The cobalt‐nitrosyl stretching vibration as a sensitive resonance Raman probe for distal histidine‐nitrosyl interaction in monomeric hemoglobins

On the Relationship of Coral Allene Oxide Synthase to Catalase

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