Literature DB >> 3689333

Haem disorder in two myoglobins: comparison of reorientation rate.

A Bellelli1, R Foon, F Ascoli, M Brunori.   

Abstract

The globins from sperm whale and from Aplysia limacina myoglobins were reconstituted by addition of stoichiometric ferric protohaem and the Soret c.d. was followed as a function of time. For both reconstituted proteins, the Soret c.d. changes with time, reflecting haem reorientation inside its pocket, as previously described [Aojula, Wilson & Drake (1986) Biochem. J. 237, 613-616] for sperm whale myoglobin. The time course of the c.d. transition is found to be approx. 10 times faster in Aplysia than in sperm whale myoglobin, a result which is in agreement with the known structural and physicochemical properties of the two myoglobins; furthermore, these results confirm that c.d. and n.m.r. data on haem orientation in haemoproteins reflect the same molecular phenomenon.

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Year:  1987        PMID： 3689333      PMCID： PMC1148347          DOI： 10.1042/bj2460787

Source DB:  PubMed          Journal:  Biochem J        ISSN： 0264-6021            Impact factor:   3.857


  13 in total

1.  Kinetic studies on the reaction between native globin and haem derivatives.

Authors:  Q H GIBSON; E ANTONINI
Journal:  Biochem J       Date:  1960-11       Impact factor: 3.857

2.  Characterization of haem disorder by circular dichroism.

Authors:  H S Aojula; M T Wilson; A Drake
Journal:  Biochem J       Date:  1986-07-15       Impact factor: 3.857

3.  Fluorescence studies of Aplysia and sperm whale apomyoglobins.

Authors:  S R Anderson; M Brunori; G Weber
Journal:  Biochemistry       Date:  1970-11-24       Impact factor: 3.162

4.  Estimation of the polarity of the protein interior by optical spectroscopy.

Authors:  R B Macgregor; G Weber
Journal:  Nature       Date:  1986 Jan 2-8       Impact factor: 49.962

5.  Proton nuclear magnetic resonance characterization of heme disorder in hemoproteins.

Authors:  G N La Mar; D L Budd; D B Viscio; K M Smith; K C Langry
Journal:  Proc Natl Acad Sci U S A       Date:  1978-12       Impact factor: 11.205

6.  Crystal structure of ferric Aplysia limacina myoglobin at 2 X 0 A resolution.

Authors:  M Bolognesi; A Coda; G Gatti; P Ascenzi; M Brunori
Journal:  J Mol Biol       Date:  1985-05-05       Impact factor: 5.469

7.  Heme orientational disorder in reconstituted and native sperm whale myoglobin. Proton nuclear magnetic resonance characterizations by heme methyl deuterium labeling in the Met-cyano protein.

Authors:  G N La Mar; N L Davis; D W Parish; K M Smith
Journal:  J Mol Biol       Date:  1983-08-25       Impact factor: 5.469

8.  Preparation and properties of apohemoglobin and reconstituted hemoglobins.

Authors:  F Ascoli; M R Fanelli; E Antonini
Journal:  Methods Enzymol       Date:  1981       Impact factor: 1.600

9.  Haem disorder in reconstituted human haemoglobin.

Authors:  J C Docherty; S B Brown
Journal:  Biochem J       Date:  1982-12-01       Impact factor: 3.857

10.  NMR study of the molecular and electronic structure of the heme cavity of Aplysia metmyoglobin. Resonance assignments based on isotope labeling and proton nuclear Overhauser effect measurements.

Authors:  U Pande; G N La Mar; J T Lecomte; F Ascoli; M Brunori; K M Smith; R K Pandey; D W Parish; V Thanabal
Journal:  Biochemistry       Date:  1986-09-23       Impact factor: 3.162
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  5 in total

1.  1H-NMR study of the effect of temperature through reversible unfolding on the heme pocket molecular structure and magnetic properties of aplysia limacina cyano-metmyoglobin.

Authors:  Zhicheng Xia; Bao D Nguyen; Maurizio Brunori; Francesca Cutruzzolà; Gerd N La Mar
Journal:  Biophys J       Date:  2005-09-08       Impact factor: 4.033

2.  Resonance Raman interrogation of the consequences of heme rotational disorder in myoglobin and its ligated derivatives.

Authors:  Freeborn Rwere; Piotr J Mak; James R Kincaid
Journal:  Biochemistry       Date:  2008-12-02       Impact factor: 3.162

3.  Haem-binding-site heterogeneity and haem Cotton effects of Glycera dibranchiata monomeric haemoglobins.

Authors:  T J DiFeo; A W Addison
Journal:  Biochem J       Date:  1989-06-15       Impact factor: 3.857

4.  Properties of a recombinant human hemoglobin with aspartic acid 99(beta), an important intersubunit contact site, substituted by lysine.

Authors:  H Yanase; S Cahill; J J Martin de Llano; L R Manning; K Schneider; B T Chait; K D Vandegriff; R M Winslow; J M Manning
Journal:  Protein Sci       Date:  1994-08       Impact factor: 6.725

5.  Complete sequence-specific 1H NMR resonance assignment of hyperfine-shifted residues in the active site of a paramagnetic protein: application to Aplysia cyano-metmyoglobin.

Authors:  J Qin; G N La Mar
Journal:  J Biomol NMR       Date:  1992-11       Impact factor: 2.835
  5 in total

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