Literature DB >> 1964590

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

M P Linhares1, L J el-Jaick, G Bemski, E Wajnberg.   

Abstract

Photolysis of HbNO has been studied from 6.2 K to 15.5 K by electron spin resonance during and after continuous illumination. Non-exponential kinetics of both dissociation and reassociation of NO was observed. The prolonged illumination separates the fast and slow ligands. This picture is consistent with NO tunnelling from two sites at different distances from the bound position. This result is obtained using a model of a sum of two exponentials or of conformational substates.

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Year:  1990        PMID: 1964590     DOI: 10.1016/0141-8130(90)90083-m

Source DB:  PubMed          Journal:  Int J Biol Macromol        ISSN: 0141-8130            Impact factor:   6.953


  2 in total

1.  Nitrosyl hemoglobin: EPR components at low temperatures.

Authors:  E Wajnberg; M P Linhares; L J el-Jaick; G Bemski
Journal:  Eur Biophys J       Date:  1992       Impact factor: 1.733

Review 2.  Contribution of Electron Paramagnetic Resonance to the studies of hemoglobin: the nitrosylhemoglobin system.

Authors:  G Bemski
Journal:  Mol Biol Rep       Date:  1997-11       Impact factor: 2.316

  2 in total

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