Resonance Raman Characterization of Soluble Guanylate Cyclase Expressed from Baculovirus

Fan, Baochen; Gupta, Garima; Danziger, Robert S.; Friedman, Joel M.; Rousseau, Denis L.

doi:10.1021/bi971934b

Cited by 34 publications

(40 citation statements)

References 32 publications

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“…Moreover, for the 5C-NO species in the ground state (Fig. 6, spectrum a) the stretching (Fe-NO) is seen at 534 cm Ϫ1 as a shoulder, as detected previously (40), which can be compared with the values obtained for other the 5C-NO proteins, 526 cm Ϫ1 for cytochrome cЈ (41) and 520 -525 cm Ϫ1 for sGC (42,43). For both species, the transient spectrum was obtained by subtracting the ground state spectrum (Ϫ5 ps) from that after photodissociation (ϩ3 ps).…”

Section: Proteinsupporting

confidence: 84%

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Role of Heme Iron Coordination and Protein Structure in the Dynamics and Geminate Rebinding of Nitric Oxide to the H93G Myoglobin Mutant

Négrerie

Kruglik

Lambry

et al. 2006

Journal of Biological Chemistry

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The influence of the heme iron coordination on nitric oxide binding dynamics was investigated for the myoglobin mutant H93G (H93G-Mb) by picosecond absorption and resonance Raman timeresolved spectroscopies. In the H93G-Mb, the glycine replacing the proximal histidine does not interact with the heme iron so that exogenous substituents like imidazole may coordinate to the iron at the proximal position. Nitrosylation of H93G-Mb leads to either 6-or 5-coordinate species depending on the imidazole concentration. At high concentrations, (imidazole)-(NO)-6-coordinate heme is formed, and the photoinduced rebinding kinetics reveal two exponential picosecond phases (ϳ10 and ϳ100 ps) similar to those of wild type myoglobin. At low concentrations, imidazole is displaced by the trans effect leading to a (NO)-5-coordinate heme, becoming 4-coordinate immediately after photolysis as revealed from the transient Raman spectrum. In this case, NO rebinding kinetics remain bi-exponential with no change in time constant of the fast component whose amplitude increases with respect to the 6-coordinate species. Bi-exponential NO geminate rebinding in 5-coordinate H93G-Mb is in contrast with the single-exponential process reported for nitrosylated soluble guanylate cyclase (Negrerie, M., Bouzhir, L., Martin, J. L., and Liebl, U. (2001) J. Biol. Chem. 276, 46815-46821). Thus, our data show that the iron coordination state or the heme iron out-of-plane motion are not at the origin of the bi-exponential kinetics, which depends upon the protein structure, and that the 4-coordinate state favors the fast phase of NO geminate rebinding. Consequently, the heme coordination state together with the energy barriers provided by the protein structure control the dynamics and affinity for NO-binding enzymes.Nitric oxide acts as a signal transmitter in several physiological pathways (1-3) because it readily diffuses through cell membranes and reacts with the heme iron. It has been proposed that the ligation of NO 2 to myoglobin has a physiological role for the in vivo regulation of the NO concentration in muscle cells (4). Numerous hemoproteins are involved in diatomic ligand binding, such as CO, O 2 , and NO, and their regulation closely depends upon the dynamic behavior of these ligands. We have shown that the dynamics of nitric oxide, and hence the geminate rebinding to the heme, are closely related to the protein function and subtly controlled by the protein structure. This control is evident when comparing endothelial NO synthase (5) and soluble guanylate cyclase (6), which are the source and the receptor of NO in cells, respectively, in which NO acts as a second messenger for signal transduction. These two proteins display a very contrasting behavior with respect to geminate rebinding of NO, which is multiphasic and relatively slow for endothelial nitric-oxide synthase, including important nanosecond phases correlated with the release of newly synthesized NO. On the other hand, NO recombination is mono-exponential and ultrafast for sGC, revealin...

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Section: Proteinsupporting

confidence: 84%

“…Bond lengths (Å) and angle for Fe-N-O in 6-and 5-coordinate porphyrin models calculated using DFT methods are compared with that from experimental high resolution x-ray structural data of NO-bound porphyrin (Por) compounds (43). BLYP indicates Becke-Lee-Yang-Parr functions.…”

Section: Table 2 Dft Calculation Of Structural Parameters For the 5-amentioning

confidence: 99%

Role of Heme Iron Coordination and Protein Structure in the Dynamics and Geminate Rebinding of Nitric Oxide to the H93G Myoglobin Mutant

Négrerie

Kruglik

Lambry

et al. 2006

Journal of Biological Chemistry

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“…2) suggests that the calculation provides a reliable guide to the character of the individual modes. This includes observed features at 507 cm -1 , 561 cm -1 , and 586 cm -1 ,associated with Fe-CO stretching and FeCO bending, as previously seen in numerous heme proteins [50][51][52][53][54][55][56][57][58][59][60]. A more detailed description of these modes, together with measurements on related compounds, will appear elsewhere.…”

Section: One-quantum Transitionsmentioning

confidence: 62%

Vibrational dynamics of biological molecules: Multi-quantum contributions

Leu

Zgierski

Wyllie

et al. 2005

Journal of Physics and Chemistry of Solids

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High-resolution X-ray measurements near a nuclear resonance reveal the complete vibrational spectrum of the probe nucleus. Because of this, nuclear resonance vibrational spectroscopy (NRVS) is a uniquely quantitative probe of the vibrational dynamics of reactive iron sites in proteins and other complex molecules. Our measurements of vibrational fundamentals have revealed both frequencies and amplitudes of 57 Fe vibrations in proteins and model compounds. Information on the direction of Fe motion has also been obtained from measurements on oriented single crystals, and provides an essential test of normal mode predictions. Here, we report the observation of weaker two-quantum vibrational excitations (overtones and combinations) for compounds that mimic the active site of heme proteins. The predicted intensities depend strongly on the direction of Fe motion. We compare the observed features with predictions based on the observed fundamentals, using information on the direction of Fe motion obtained either from DFT predictions or from single crystal measurements. Two-quantum excitations may become a useful tool to identify the directions of the Fe oscillations when single crystals are not available.

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“…However, neither the Fe-His nor the Fe-imidazole stretching band was identified. This spectrum is reminiscent of sGC1 [8,9]. These observations suggest that 1.2 M imidazole denatured sGC to allow autoxidation, yielding a mixture of 5c-and 6c-hemes.…”

Section: Resultsmentioning

confidence: 83%

“…The native sGC as isolated from bovine lung stays in the reduced state and contains five-coordinated (5c) high-spin (HS) heme, ligated by a conserved histidine (His) residue at position 105 (rat lung protein) on b-subunit [6,7]. However, two other groups independently found sGC as a mixture of 5c-HS and sixcoordinated (6c) low-spin (LS) species [8,9]. The latter enzyme is categorized as sGC1 to distinguish from the former which is categorized as sGC2.…”

Section: Introductionmentioning

confidence: 99%

Resonance Raman study on synergistic activation of soluble guanylate cyclase by imidazole, YC-1 and GTP

Pal¹,

Li²,

Ohta³

et al. 2004

Journal of Inorganic Biochemistry

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Resonance Raman Characterization of Soluble Guanylate Cyclase Expressed from Baculovirus

Cited by 34 publications

References 32 publications

Role of Heme Iron Coordination and Protein Structure in the Dynamics and Geminate Rebinding of Nitric Oxide to the H93G Myoglobin Mutant

Role of Heme Iron Coordination and Protein Structure in the Dynamics and Geminate Rebinding of Nitric Oxide to the H93G Myoglobin Mutant

Vibrational dynamics of biological molecules: Multi-quantum contributions

Resonance Raman study on synergistic activation of soluble guanylate cyclase by imidazole, YC-1 and GTP

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