Single crystal EPR study of the Ni center of NiFe hydrogenase

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 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.