An EPR/HYSCORE, Mössbauer, and resonance Raman study of the hydrogenase maturation enzyme HydF: a model for N-coordination to [4Fe–4S] clusters

@article{Berggren2013AnEM,
  title={An EPR/HYSCORE, M{\"o}ssbauer, and resonance Raman study of the hydrogenase maturation enzyme HydF: a model for N-coordination to [4Fe–4S] clusters},
  author={Gustav Berggren and Ricardo Garc{\'i}a-Serres and Xavier Brazzolotto and Martin Cl{\'e}mancey and Serge Gambarelli and Mohamed Abou El Atta and Jean-Marc Latour and Heather L. Hern{\'a}ndez and Sowmya Subramanian and Michael K. Johnson and Marc Fontecave},
  journal={JBIC Journal of Biological Inorganic Chemistry},
  year={2013},
  volume={19},
  pages={75-84}
}
The biosynthesis of the organometallic H cluster of [Fe–Fe] hydrogenase requires three accessory proteins, two of which (HydE and HydG) belong to the radical S-adenosylmethionine enzyme superfamily. The third, HydF, is an Fe–S protein with GTPase activity. The [4Fe–4S] cluster of HydF is bound to the polypeptide chain through only the three, conserved, cysteine residues present in the binding sequence motif CysXHisX(46-53)HisCysXXCys. However, the involvement of the two highly conserved… CONTINUE READING
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