Multifrequency EPR studies on the Mn(II) centers of oxalate decarboxylase

被引:31
作者
Angerhofer, Alexander
Moomaw, Ellen W.
Garcia-Rubio, Ines
Ozarowski, Andrew
Krzystek, J.
Weber, Ralph T.
Richards, Nigel G. J.
机构
[1] Univ Florida, Dept Chem, Gainesville, FL 32611 USA
[2] ETH, Phys Chem Lab, CH-8043 Zurich, Switzerland
[3] Florida State Univ, Natl High Magnet Field Lab, Tallahassee, FL 32310 USA
[4] Bruker Biospin Corp, Billerica, MA 01821 USA
关键词
D O I
10.1021/jp0715326
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
Oxalate decarboxylase from Bacillus subtilis is composed of two cupin domains, each of which contains a Mn(II) ion coordinated by four identical conserved residues. The similarity between the two Mn(II) sites has precluded previous attempts to distinguish them spectroscopically and complicated efforts to understand the catalytic mechanism. A multifrequency cw-EPR approach has now enabled us to show that the two Mn ions can be distinguished on the basis of their differing fine structure parameters and to observe that acetate and formate bind to Mn(II) in only one of the two sites. The EPR evidence is consistent with the hypothesis that this Mn-binding site is located in the N-terminal domain, in agreement with predictions based on a recent X-ray structure of the enzyme.
引用
收藏
页码:5043 / 5046
页数:4
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