Rationally engineered flavin-dependent oxidase reveals steric control of dioxygen reduction.

@article{Zafred2015RationallyEF,
  title={Rationally engineered flavin-dependent oxidase reveals steric control of dioxygen reduction.},
  author={Domen Zafred and Barbara Steiner and Andrea R Teufelberger and Altijana Hromic and P. Andrew Karplus and Christopher J. Schofield and Silvia Wallner and Peter Macheroux},
  journal={The FEBS journal},
  year={2015},
  volume={282 16},
  pages={
          3060-74
        }
}
UNLABELLED The ability of flavoenzymes to reduce dioxygen varies greatly, and is controlled by the protein environment, which may cause either a rapid reaction (oxidases) or a sluggish reaction (dehydrogenases). Previously, a 'gatekeeper' amino acid residue was identified that controls the reactivity to dioxygen in proteins from the vanillyl alcohol oxidase superfamily of flavoenzymes. We have identified an alternative gatekeeper residue that similarly controls dioxygen reactivity in the grass… CONTINUE READING
Related Discussions
This paper has been referenced on Twitter 3 times. VIEW TWEETS

References

Publications referenced by this paper.
Showing 1-10 of 34 references

family sharing a conserved FAD-binding domain

D Zafred, A Nandy, L Pump, H Kahlert, W Keller
Trends Biochem. Sci • 2013

Berberine bridge enzyme and the family

S Wallner, C Dully, B Daniel, P Macheroux
2012