Dj. Hopper et J. Rogozinski, REDOX POTENTIAL OF THE HEME-C GROUP IN THE QUINOCYTOCHROME, LUPANINE HYDROXYLASE, AN ENZYME LOCATED IN THE PERIPLASM OF A PSEUDOMONAS SP, Biochimica et biophysica acta. Protein structure and molecular enzymology, 1383(1), 1998, pp. 160-164
The quinocytochrome c, lupanine hydroxylase, was shown to be located i
n the periplasm of a Pseudomonas sp. The midpoint redox potential of t
he haem In the purified enzyme was measured by potentiometric titratio
n and shown to be +193 mV. PQQ was removed from the enzyme by isoelect
ric focusing to give inactive apoenzyme. This resulted in a shift in t
he midpoint redox potential of the haem to +98 mV. Full activity was r
ecovered by the addition of PQQ to apoenzyme that also restored the or
iginal potential. (C) 1998 Elsevier Science B.V.