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Literature DB >> 9414233

Temperature dependence of Q-band electron paramagnetic resonance spectra of nitrosyl heme proteins.

Abstract

The Q-band (35 GHz) electron paramagnetic resonance (EPR) spectra of nitrosyl hemoglobin (HbNO) and nitrosyl myoglobin (MbNO) were studied as a function of temperature between 19 K and 200 K. The spectra of both heme proteins show two classes of variations as a function of temperature. The first one has previously been associated with the existence of two paramagnetic species, one with rhombic and the other with axial symmetry. The second one manifests itself in changes in the g-factors and linewidths of each species. These changes are correlated with the conformational substates model and associate the variations of g-values with changes in the angle of the N(his)-Fe-N(NO) bond in the rhombic species and with changes in the distance between Fe and N of the proximal (F8) histidine in the axial species.

Entities: Chemical

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Year: 1997 PMID： 9414233 PMCID： PMC1181224 DOI： 10.1016/S0006-3495(97)78347-4

Source DB: PubMed Journal: Biophys J ISSN： 0006-3495 Impact factor: 4.033

22 in total

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Authors: M Chevion; A Stern; J Peisach; W E Blumberg; S Simon
Journal: Biochemistry Date: 1978-05-02 Impact factor: 3.162

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Authors: E Wajnberg; G Bemski; L J el-Jaick; O C Alves
Journal: Int J Biol Macromol Date: 1996-04 Impact factor: 6.953

3. An ESR study of nitrosyl-Aplysia brasiliana myoglobin and nitrosyl annelidae Glossoscolex paulistus erythrocruorin.

Authors: I Caracelli; N C Meirelles; M Tabak; O Baffa Filho; O R Nascimento
Journal: Biochim Biophys Acta Date: 1988-08-10

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Authors: T Shiga; K J Hwang; I Tyuma
Journal: Biochemistry Date: 1969-01 Impact factor: 3.162

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Authors: R H Morse; S I Chan
Journal: J Biol Chem Date: 1980-08-25 Impact factor: 5.157

6. Dynamics of ligand binding to myoglobin.

Authors: R H Austin; K W Beeson; L Eisenstein; H Frauenfelder; I C Gunsalus
Journal: Biochemistry Date: 1975-12-02 Impact factor: 3.162

7. Origin of observed changes in 14N hyperfine interaction accompanying R leads to T transition in nitrosylhemoglobin.

Authors: S K Mun; J C Chang; T P Das
Journal: Proc Natl Acad Sci U S A Date: 1979-10 Impact factor: 11.205

8. Influence of globin structures on the state of the heme. Ferrous low spin derivatives.

Authors: M F Perutz; J V Kilmartin; K Nagai; A Szabo; S R Simon
Journal: Biochemistry Date: 1976-01-27 Impact factor: 3.162

9. Single crystal EPR of myoglobin nitroxide. Freezing-induced reversible changes in the molecular orientation of the ligand.

Authors: H Hori; M Ikeda-Saito; T Yonetani
Journal: J Biol Chem Date: 1981-08-10 Impact factor: 5.157

Temperature dependence of Q-band electron paramagnetic resonance spectra of nitrosyl heme proteins.

1. Analogous effect of protons and inositol hexaphosphate on the alteration of structure of nitrosyl fetal human hemoglobin.

2. Nitrosyl hemoglobins: EPR above 80 K.

3. An ESR study of nitrosyl-Aplysia brasiliana myoglobin and nitrosyl annelidae Glossoscolex paulistus erythrocruorin.

4. Electron paramagnetic resonance studies of nitric oxide hemoglobin derivatives. I. Human hemoglobin subunits.

5. Electron paramagnetic resonance studies of nitrosyl ferrous heme complexes. Determination of an equilibrium between two conformations.

6. Dynamics of ligand binding to myoglobin.

7. Origin of observed changes in 14N hyperfine interaction accompanying R leads to T transition in nitrosylhemoglobin.

8. Influence of globin structures on the state of the heme. Ferrous low spin derivatives.

9. Single crystal EPR of myoglobin nitroxide. Freezing-induced reversible changes in the molecular orientation of the ligand.

10. EPR spectral changes of nitrosyl hemes and their relation to the hemoglobin T-R transition.

1. Proton electron nuclear double resonance from nitrosyl horse heart myoglobin: the role of His-E7 and Val-E11.

2. Differential sensing of protein influences by NO and CO vibrations in heme adducts.

3. EPR spectroscopy of nitrite complexes of methemoglobin.

4. Amyloid β chaperone - lipocalin-type prostaglandin D synthase acts as a peroxidase in the presence of heme.

5. EPR characterisation of the ferrous nitrosyl complex formed within the oxygenase domain of NO synthase.