Abstract
Pyrococcus furiosus glyceraldehyde 3-phosphate oxidoreductase has been characterized using EPR-monitored redox titrations. Two different W signals were found. W1/5+ is an intermediate species in the catalytic cycle, with the midpoint potentials E(m)(W(6+/5+)) = -507 mV and E(m)(W(5+/4+)) = -491 mV. W2/5+ represents an inactivated species with E(m)(W(6+/5+)) = -329 mV. The cubane cluster exhibits both S = 3/2 and S = 1/2 signals with the same midpoint potential: E(m)([4Fe-4S](2+/1+)) = -335 mV. The S = 1/2 EPR signal is unusual with all g values below 2.0. The titration results combined with catalytic voltammetry data are consistent with electron transfer from glyceraldehyde 3-phosphate first to the tungsten center, then to the cubane cluster and finally to the ferredoxin.
Original language | English |
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Pages (from-to) | 66-70 |
Journal | FEBS Letters |
Volume | 462 |
Issue number | 1-2 |
DOIs | |
Publication status | Published - 1999 |
Externally published | Yes |
Keywords
- Electron paramagnetic resonance
- Glyceraldehyde 3-phosphate oxidoreductase
- Pyrococcus furiosus
- Reduction potential
- Tungsten