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Interaction between external medium and haem pocket in myoglobin probed by low-temperature optical spectroscopy.

Abstract：

:The visible absorption spectra of carbonmonoxymyoglobin in the temperature range 300 to 20 K are reported and compared with the analogous spectra of carbonomonoxyhaemoglobin. The temperature dependence of the zeroth, first and second moment of the observed bands is analysed to obtain information on the local dynamics in the proximity of the haem. Contrary to haemoglobin, the first moment of the observed bands in myoglobin is markedly affected by the solvent composition and its value saturates at temperatures at which the solvent undergoes the glass transition. These data indicate that solvent properties influence the haem pocket stereodynamics in myoglobin; moreover, the different behaviour between myoglobin and haemoglobin suggests that the process should involve the surfaces that are buried in the haemoglobin tetramer and exposed to the solvent in myoglobin, and/or the different protein compressibility.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Cordone L,Cupane A,Leone M,Vitrano E,Bulone D

doi

10.1016/0022-2836(88)90390-7

subject

Has Abstract

pub_date

1988-01-05 00:00:00

pages

213-8

issue

1

eissn

0022-2836

issn

1089-8638

pii

0022-2836(88)90390-7

journal_volume

199

pub_type

杂志文章

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