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**Nota de Física****Publicado**

# **Proton Electron Nuclear Double Resonance from Nitrosyl Horse Heart Myoglobin: The Role of His-E7 and Val-E11**

**Marco Flores; Eliane Wajnberg; G. Bemski**

1999

[**Descargar PDF **0,2 MB](https://index.cbpf.br/files/publicacao/6ad2a767639f62b11adbb45b/pdf) [**Contactar al responsable**](mailto:apub@cbpf.br?subject=Proton%20Electron%20Nuclear%20Double%20Resonance%20from%20Nitrosyl%20Horse%20Heart%20Myoglobin%3A%20The%20Role%20of%20His-E7%20and%20Val-E11)

## **Datos de la publicación**

<dl>

<dt>Autores</dt>
<dd>Marco Flores; Eliane Wajnberg; G. Bemski</dd>

<dt>Tipo</dt>
<dd>Nota de Física</dd>

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

<dt>Fecha de publicación</dt>
<dd>1999</dd>

<dt>Descripción</dt>
<dd>Electron Nuclear Double Resonance (ENDOR) spectroscopy has been used to study protons in nitrosyl horse heart myoglobin (MbNO). &lt;math&gt; ^1H\,\!&lt;/math&gt; ENDOR spectra were recorded for different settings of the magnetic field. Detailed analysis of the ENDOR powder spectra using computer simulation, based on the “orientation-selection” principle lead to the identification of the available protons in the heme pocket. We observe hyperfine interactions of the &lt;math&gt;N(HisF8)-Fe^{2+}-N (NO)\,\!&lt;/math&gt; complex with five protons in axial and with eight protons in the rhombic symmetry along different orientations including those of the principal axes of the g-tensor. Protons from His-E7 and Val-E11 residues are identified in the two symmetries, rhombic and axial, exhibited by MbNO. Our results indicate that both residues are present inside the heme pocket and help to stabilize one particular conformation.</dd>

<dt>Año</dt>
<dd>1999</dd>

<dt>Número</dt>
<dd>CBPF-NF-034/99</dd>

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

<dt>Vínculo con beca</dt>
<dd>No</dd>

</dl>

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```

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