✍ Scribed by Ch. Geßner; O. Trofanchuk; K. Kawagoe; Y. Higuchi; N. Yasuoka; W. Lubitz
No coin nor oath required. For personal study only.
EPR spectra of single crystals of NiFe hydrogenase from Desulfovibrio vulgaris Miyazaki F were evaluated and yielded the g-tensors of the Ni center for two different states of the enzyme. The g-values associated with these states are identical to those measured in frozen solutions for the ready (Ni-B) and the unready (Ni-A) form of the Ni center. Directions of the g-tensor axes were determined relative to the crystal symmetry axes. The obtained changes of g-values and tensor axes orientations between Ni-A and Ni-B can be explained by a structural difference involving modification of a cysteine sulfur ligand.
📜 SIMILAR VOLUMES
The EPR of Gd3' in PrF3 has been observed to be consistent with the C2v symmetry of the fad crystallirle field, but the linewidths show an unusual variation along a fixed direction. The orientation of the Y axis of the spectrum convincingly supports the C& structure for the crystat and not the Dfd s