Single crystal EPR studies of the oxidized active site of [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F

被引：0

作者：

O. Trofanchuk

M. Stein

Ch. Geßner

F. Lendzian

Y. Higuchi

W. Lubitz

机构：

[1] Max-Volmer-Institut für Biophysikalische Chemie und Biochemie,

[2] Technische Universität Berlin,undefined

[3] D-10623 Berlin,undefined

[4] Germany e-mail: lubitz@struktur.chem.tu-berlin.de Fax: +49-30-31421122,undefined

[5] Division of Chemistry,undefined

[6] Graduate School of Science Kyoto University,undefined

[7] Sakyo-ku,undefined

[8] Kyoto 606-01,undefined

[9] Japan,undefined

来源：

JBIC Journal of Biological Inorganic Chemistry | 2000年 / 5卷

关键词：

Key words Nickel-iron hydrogenase; Single crystal electron paramagnetic resonance; g-Tensor; Electronic structure;

D O I：

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学科分类号：

摘要：

The Ni-A and the Ni-B forms of the [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F have been studied in single crystals by continuous wave and pulsed EPR spectroscopy at different temperatures (280 K, 80 K, and 10 K). For the first time, the orientation of the g-tensor axes with respect to the recently published atomic structure of the active site at 1.8 Å resolution was elucidated for Ni-A and Ni-B. The determined g-tensors have a similar orientation. The configuration of the electronic ground state is proposed to be Ni(III) 3d1z2 for Ni-A and Ni-B. The gz principal axis is close to the Ni-S(Cys549) direction; the gx and the gy axes are approximately along the Ni-S(Cys546) and Ni-S(Cys81) bonds, respectively. It is proposed that the difference between the Ni-A and Ni-B states lies in a protonation of the bridging ligand between the Ni and the Fe.

引用

页码：36 / 44

页数：8