---
title: "Spin-Lattice Relaxation of Denatured Nitrosyl Hemoproteins • CBPF Index"
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**Nota de Física****Publicado**

# **Spin-Lattice Relaxation of Denatured Nitrosyl Hemoproteins**

**Eliane Wajnberg; O. C. Alves**

1996

[**Descargar PDF **0,5 MB](https://index.cbpf.br/files/publicacao/6ad2a767639f62b11adbb522/pdf) [**Contactar al responsable**](mailto:apub@cbpf.br?subject=Spin-Lattice%20Relaxation%20of%20Denatured%20Nitrosyl%20Hemoproteins)

## **Datos de la publicación**

<dl>

<dt>Autores</dt>
<dd>Eliane Wajnberg; O. C. Alves</dd>

<dt>Tipo</dt>
<dd>Nota de Física</dd>

<dt>Estado</dt>
<dd>Publicado</dd>

<dt>Fecha de publicación</dt>
<dd>1996</dd>

<dt>Descripción</dt>
<dd>The temperature dependence of spin-lattice relaxation (SLR) for denatured nitrosyl hemoglobin (HbNO) and nitrosyl Myoglobin (MbNO), powdered HbNO and hematin-NO was studied in the range from 4K to 70K. The results were fitted with both &lt;math&gt; T^{n}\,\!&lt;/math&gt; and &lt;math&gt; e^{-\Delta/T}\,\!&lt;/math&gt; models. In the first one the relaxation is mediated by tunneling modes of a two level system. We observed a correlation between the n values and the functional state of protein. The stricking coincidence of the range of the low lying energy level and the temperature range where EPR spectra changes suggest the existence of two conformation of the liganded heme. The relevance of the presence and structure of the globin is revealed itself in the difference between parameters determined for native, hematin and denatured proteins.</dd>

<dt>Año</dt>
<dd>1996</dd>

<dt>Número</dt>
<dd>CBPF-NF-003/96</dd>

<dt>Vínculo con tesis</dt>
<dd>No</dd>

<dt>Vínculo con beca</dt>
<dd>No</dd>

</dl>

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