X-ray absorption and resonance Raman studies of methyl-coenzyme M reductase indicating that ligand exchange and macrocycle reduction accompany reductive activation.

@article{Tang2002XrayAA,
  title={X-ray absorption and resonance Raman studies of methyl-coenzyme M reductase indicating that ligand exchange and macrocycle reduction accompany reductive activation.},
  author={Qun Tang and Paul E. Carrington and Y Y Horng and Michael J Maroney and Stephen W Ragsdale and David F Bocian},
  journal={Journal of the American Chemical Society},
  year={2002},
  volume={124 44},
  pages={13242-56}
}
Methyl-coenzyme M reductase (MCR) catalyzes methane formation from methyl-coenzyme M (methyl-SCoM) and N-7-mercaptoheptanoylthreonine phosphate (CoBSH). MCR contains a nickel hydrocorphin cofactor at its active site, called cofactor F(430). Here we present evidence that the macrocyclic ligand participates in the redox chemistry involved in catalysis. The active form of MCR, the red1 state, is generated by reducing another spectroscopically distinct form called ox1 with titanium(III) citrate… CONTINUE READING
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