Journal
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
Volume 5, Issue 6, Pages 682-691Publisher
SPRINGER-VERLAG
DOI: 10.1007/s007750000152
Keywords
hydrogenase; metalloenzyme; nickel enzyme; iron-sulfur center; catalytic cycle
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The question of the existence of a rate-limiting step in the catalytic cycle of Ni-Fe hydrogenases was taken up by using the sets of data available in the case of two specific enzymes: the hydrogenase from Thiocapsa roseopercisina, in which isotope effects have been systematically investigated over a wide pH range, and the enzyme from Desulfovibrio fructosovorans , for which the activities and the redox properties have been studied in two different forms, the wild type and the P238C mutant. When these data are analyzed in the light of appropriate kinetic models, it is concluded that electron transfer and proton transfer are rate limiting in the H-2 uptake and H-2 evolution reactions, respectively. This proposal is consistent with the data available from other Ni-Fe enzymes.
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