Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Nitrosyl hemoglobin: EPR components at low temperatures.

Literature DB >> 1325345

Nitrosyl hemoglobin: EPR components at low temperatures.

E Wajnberg¹, M P Linhares, L J el-Jaick, G Bemski.

Abstract

The EPR spectrum of nitrosyl hemoglobin has been studied from 7.5 K to 104 K. It is composed of at least three components (A, B and C) which have a different dependence on temperature and power level. The A component decreases with increasing temperature. The B component disappears at around 30 K and is replaced by C. Relaxation of A follows the Orbach mechanism with an energy of 28 cm-1. This behavior can be attributed to phonon induced changes in the orientation of NO with respect to the heme plane.

Entities: Chemical

Mesh：

Substances：

Year: 1992 PMID： 1325345 DOI： 10.1007/bf00195444

Source DB: PubMed Journal: Eur Biophys J ISSN： 0175-7571 Impact factor: 1.733

24 in total

Review 1. Allosteric interpretation of haemoglobin properties.

Authors: R G Shulman; J J Hopfield; S Ogawa
Journal: Q Rev Biophys Date: 1975-07 Impact factor: 5.318

2. E.p.r. studies of photolysis of nitrosyl haemoglobin at low temperatures.

Authors: M P Linhares; L J el-Jaick; G Bemski; E Wajnberg
Journal: Int J Biol Macromol Date: 1990-02 Impact factor: 6.953

3. The mechanism of reaction of nitrosyl with met- and oxymyoglobin: an ESR study.

Authors: L M Neto; O R Nascimento; M Tabak; I Caracelli
Journal: Biochim Biophys Acta Date: 1988-09-21

4. Electron paramagnetic studies of nitric oxide haemoglobin derivatives: isolated subunits and nitric oxide hybrids.

Authors: Y Henry; R Banerjee
Journal: J Mol Biol Date: 1973-02-05 Impact factor: 5.469

5. Chain non-equivalence in nitric oxide binding to hemoglobin.

Authors: Y Henry; R Cassoly
Journal: Biochem Biophys Res Commun Date: 1973-04-02 Impact factor: 3.575

6. Determination of the zero-field splitting of Fe 3+ in heme proteins from the temperature dependence of the spin-lattice relaxation rate.

Authors: C P Scholes; R A Isaacson; G Feher
Journal: Biochim Biophys Acta Date: 1971-07-20

7. Structure of nitric oxide hemoglobin.

Authors: J F Deatherage; K Moffat
Journal: J Mol Biol Date: 1979-11-05 Impact factor: 5.469

8. Ultrafast relaxation in picosecond photolysis of nitrosylhemoglobin.

Authors: P A Cornelius; R M Hochstrasser; A W Steele
Journal: J Mol Biol Date: 1983-01-05 Impact factor: 5.469

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

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

Nitrosyl hemoglobin: EPR components at low temperatures.

Review 1. Allosteric interpretation of haemoglobin properties.

2. E.p.r. studies of photolysis of nitrosyl haemoglobin at low temperatures.

3. The mechanism of reaction of nitrosyl with met- and oxymyoglobin: an ESR study.

4. Electron paramagnetic studies of nitric oxide haemoglobin derivatives: isolated subunits and nitric oxide hybrids.

5. Chain non-equivalence in nitric oxide binding to hemoglobin.

6. Determination of the zero-field splitting of Fe 3+ in heme proteins from the temperature dependence of the spin-lattice relaxation rate.

7. Structure of nitric oxide hemoglobin.

8. Ultrafast relaxation in picosecond photolysis of nitrosylhemoglobin.

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

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

Review 1. Contribution of Electron Paramagnetic Resonance to the studies of hemoglobin: the nitrosylhemoglobin system.

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

3. Oxygen and CO binding to triply NO and asymmetric NO/CO hemoglobin hybrids.

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