Literature DB >> 4508147

Coboglobins: cobalt substitution and the nature of the prosthetic group--apoprotein interaction in hemoglobin and myoglobin.

B M Hoffman, C A Spilburg, D H Petering.   

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Year:  1972        PMID： 4508147     DOI： 10.1101/sqb.1972.036.01.045

Source DB:  PubMed          Journal:  Cold Spring Harb Symp Quant Biol        ISSN： 0091-7451


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  6 in total

1.  Redox equilibria of liganded forms of methemoglobin.

Authors:  C Bull; B M Hoffman
Journal:  Proc Natl Acad Sci U S A       Date:  1975-09       Impact factor: 11.205

2.  Emission Mössbauer study of the stereochemical trigger that initiates cooperative interaction of hemoglobin subunits.

Authors:  T S Srivastava; S Tyagi; A Nath
Journal:  Proc Natl Acad Sci U S A       Date:  1977-11       Impact factor: 11.205

3.  Electron paramagnetic resonance of single crystal oxycobaltmyoglobin and deoxycobaltmyoglobin.

Authors:  J C Chien; L C Dickinson
Journal:  Proc Natl Acad Sci U S A       Date:  1972-10       Impact factor: 11.205

4.  Stereochemical trigger for initiating cooperative interaction of the subunits during the oxygenation of cobaltohemoglobin.

Authors:  J L Hoard; W R Scheidt
Journal:  Proc Natl Acad Sci U S A       Date:  1973-12       Impact factor: 11.205

5.  Coboglobins: heterotropic linkage and the existence of a quaternary structure change upon oxygenation of cobaltohemoglobin.

Authors:  G C Hsu; C A Spilburg; C Bull; B M Hoffman
Journal:  Proc Natl Acad Sci U S A       Date:  1972-08       Impact factor: 11.205

6.  Formation of bile pigments by coupled oxidation of cobalt-substituted haemoglobin and myoglobin.

Authors:  D I Vernon; S B Brown
Journal:  Biochem J       Date:  1984-10-01       Impact factor: 3.857
  6 in total

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