Characterization of D. desulfuricans (ATCC 27774) [NiFe] hydrogenase EPR and redox properties of the native and the dihydrogen reacted states.
Redox intermediates of D. desulfuricans ATCC 27774 [NiFe] hydrogenase were generated under dihydrogen. Detailed redox titrations, coupled to EPR measurements, give access to the mid-point redox potentials of the iron-sulfur centers and of the Nickel-B signal that represents the ready form of the enzyme. The interaction between the dihydrogen molecule and the nickel centre was probed by the observation of an isotopic effect on the EPR signals detected in turnover conditions, by comparison of the H2O/H2 and D2O/D2-reacted samples.
Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, Monte de Caparica, Portugal.
R
R
Franco
I
I
Moura
J
J
LeGall
H D
HD
Peck
B H
BH
Huynh
J J
JJ
Moura
D001665:Binding Sites; D003901:Desulfovibrio / Q000201:enzymology* / Q000235:genetics; D004574:Electromagnetic Fields; D004578:Electron Spin Resonance Spectroscopy; D006864:Hydrogenase / Q000737:chemistry*; D010084:Oxidation-Reduction; D013696:Temperature
C043296:nickel-iron hydrogenase; D006864:Hydrogenase