| Literature DB >> 16133204 |
Boris Epel1, Kai-Oliver Schäfer, Armin Quentmeier, Cornelius Friedrich, Wolfgang Lubitz.
Abstract
A detailed analysis of the EPR signatures at X-band and Q-band of an enzyme (SoxB) involved in sulfur oxidation from Paracoccus pantotrophus is presented. EPR spectra are attributed to an exchange-coupled dimanganese Mn(2)(II,II) complex. An antiferromagnetic exchange interaction of J=-7.0 (+/-1) cm(-1) (H=-2JS ( 1 ) S ( 2 )) is evidenced by a careful examination of the temperature dependence of the EPR spectra. The spin Hamiltonian parameters for a total spin of S ( T ) =1, 2 and 3 are obtained and an inter-manganese distance of 3.4 (+/-0.1) A is estimated. The comparison with exchange coupling and inter-manganese distance data of other dimanganese proteins and model compounds leads to a tentative assignment of the Mn bridging ligands to bis(mu-hydroxo) (mu-carboxylato).Entities:
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Year: 2005 PMID: 16133204 DOI: 10.1007/s00775-005-0015-3
Source DB: PubMed Journal: J Biol Inorg Chem ISSN: 0949-8257 Impact factor: 3.358