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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Redox chemistry of cobalamin and iron-sulfur cofactors in the tetrachloroethene reductase of Dehalobacter restrictus.

Respiration of Dehalobacter restrictus is based on reductive dechlorination of tetrachloroethene. The terminal component of the respiratory chain is the membrane-bound tetrachloroethene reductase. The metal prosthetic groups of the purified enzyme have been studied by optical and EPR spectroscopy. The 60-kDa monomer contains one cobalamin with Em(Co[1+/2+]) = -350 mV and Em(Co[2+/3+]) > 150 mV and two electron-transferring [4Fe-4S](2+;1+) clusters with rather low redox potentials of Em approximately -480 mV. The cob(II)alamin is present in the base-off configuration. A completely reduced enzyme sample reacted very rapidly with tetrachloroethene yielding base-off cob(II)alamin rather than trichlorovinyl-cob(III)alamin.[1]

References

  1. Redox chemistry of cobalamin and iron-sulfur cofactors in the tetrachloroethene reductase of Dehalobacter restrictus. Schumacher, W., Holliger, C., Zehnder, A.J., Hagen, W.R. FEBS Lett. (1997) [Pubmed]
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