Literature DB >> 4655252

Flavine-protein interactions in flavoenzymes. Temperature-jump and stopped-flow studies of flavine analog binding to the apoprotein of Azotobacter flavodoxin.

B G Barman, G Tollin.   

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Year:  1972        PMID： 4655252     DOI： 10.1021/bi00775a018

Source DB:  PubMed          Journal:  Biochemistry        ISSN： 0006-2960            Impact factor:   3.162


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  5 in total

1.  The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate.

Authors:  C P van Mierlo; W M van Dongen; F Vergeldt; W J van Berkel; E Steensma
Journal:  Protein Sci       Date:  1998-11       Impact factor: 6.725

2.  Apoflavodoxin (un)folding followed at the residue level by NMR.

Authors:  C P van Mierlo; J M van den Oever; E Steensma
Journal:  Protein Sci       Date:  2000-01       Impact factor: 6.725

3.  Covalently bound non-coenzyme phosphorus residues in flavoproteins: 31P nuclear magnetic resonance studies of Azotobacter flavodoxin.

Authors:  D E Edmondson; T L James
Journal:  Proc Natl Acad Sci U S A       Date:  1979-08       Impact factor: 11.205

Review 4.  Structure-function relations in flavodoxins.

Authors:  R P Simondsen; G Tollin
Journal:  Mol Cell Biochem       Date:  1980-12-10       Impact factor: 3.396

5.  Kinetics and thermodynamics of the binding of riboflavin, riboflavin 5'-phosphate and riboflavin 3',5'-bisphosphate by apoflavodoxins.

Authors:  J J Pueyo; G P Curley; S G Mayhew
Journal:  Biochem J       Date:  1996-02-01       Impact factor: 3.857
  5 in total

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