Nickel hydrogenases ENDOR studies

Fe Q-band ENDOR study of the isotopically enriched Ni-C state of D. gigas and D. desulfuricans hydrogenases and Ni-B state of D. desulfuricans revealed a weak coupling between the Fe and the nickel atoms when the enzyme was in the Ni-A forms while no coupling was observed for the Ni-B form (186). A careful analysis of linewidth of Ni-A and Ni-B EPR signals detected in Fe enriched and nonenriched hydrogenase samples indicated that hyperfine interactions are lost in the spectral linewidth and, hence, nonde-tectable. [Pg.394]

Fan, C. L., Teixeira, M., Moura, J., Moura, I., Huynh, B. H., Legall, J., Peck, H. D. and Hoffman, B. M. (1991) Detection and characterization of exchangeable protons bound to the hydrogen-activation nickel site of Desulfovibrio gigas hydrogenase - a H-1 and H-2 Q-band ENDOR study./. Amer. Chem. Soc., 113, 1-24... [Pg.262]

Fan C,Teixeira M, Moura J, et al. 1991. Detection and characterization of exchangeable protons bound to the hydrogen-activating nickel site of Desulfovibrio gigas hydrogenase a and Q-band ENDOR study. J Am Chem Soc 113 20. ... [Pg.32]

Fan C, Teixeira M, Moura JJG, Moura I, Huynh BH, LeGall J, Peck Jr HD, Hofftnan BM. 1991. Detection and characterisation of exchangable protons bound to the hydrogen-activation nickel site of desulfovibrio gigas hydrogenase a H and H Q-Band ENDOR study. JAm Chem Soc 113 20-24. [Pg.470]

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