Control of oxidation-reduction potentials in flavodoxin from Clostridium beijerinckii: the role of conformation changes.

@article{Ludwig1997ControlOO,
  title={Control of oxidation-reduction potentials in flavodoxin from Clostridium beijerinckii: the role of conformation changes.},
  author={Martha L. Ludwig and Katherine A. Pattridge and Allan L. Metzger and Melinda M. Dixon and Mine Eren and Y Feng and Richard P Swenson},
  journal={Biochemistry},
  year={1997},
  volume={36 6},
  pages={1259-80}
}
X-ray analyses of wild-type and mutant flavodoxins from Clostridium beijerinckii show that the conformation of the peptide Gly57-Asp58, in a bend near the isoalloxazine ring of FMN, is correlated with the oxidation state of the FMN prosthetic group. The Gly-Asp peptide may adopt any of three conformations: trans O-up, in which the carbonyl oxygen of Gly57 (O57) points toward the flavin ring; trans O-down, in which O57 points away from the flavin; and cis O-down. Interconversions among these… CONTINUE READING
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