Module fusion in an A-type flavoprotein from the cyanobacterium Synechocystis condenses a multiple-component pathway in a single polypeptide chain

Author:

Vicente João B.,Gomes Cláudio M.,Wasserfallen Alain,Teixeira Miguel

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference24 articles.

1. A family of flavoproteins in the domains Archaea and Bacteria;Wasserfallen;Eur. J. Biochem.,1998

2. Studies on the redox centers of the terminal oxidase from Desulfovibrio gigas and evidence for its interaction with rubredoxin;Gomes;J. Biol. Chem.,1997

3. C.M. Gomes, M. Teixeira, A. Wasserfallen, in: S. Ghisla, P.K. Kroneck, P. Macheroux, H. Sund (Eds.), The Family of A-type Flavoproteins New Members and Definition of Unique Sequence Fingerprints, Rudolf Weber-Agency for Scientific Publications, Berlin, 1999

4. Spectroscopic studies and characterization of a novel electron-transfer chain from Escherichia coli involving a flavorubredoxin and its flavoprotein reductase partner;Gomes;Biochemistry,2000

5. Structure of a dioxygen reduction enzyme from Desulfovibrio gigas;Frazão;Nat. Struct. Biol.,2000

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