BMB Reports
- Volume 31 Issue 5
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- Pages.444-452
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- 1998
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- 1976-670X(eISSN)
Redox Potential of a Soybean Ferric Leghemoglobin Reductase
- Kim, Hyun-Mi (Department of Biochemistry, Natural Science Research Institute, Yonsei University)
- Received : 1998.05.06
- Accepted : 1998.06.03
- Published : 1998.09.30
Abstract
The visible spectra of soybean ferric leghemoglobin reductase exhibited a charge transfer band at 530 nm under aerobic condition. Spectra of the oxidized enzyme show a flavin peak at 454 nm and the enzyme has three redox states associated with the active site of the enzyme. The enzyme has an active disulfide bridge and two-electron transfer may dominate in the ferric state of leghemoglobin reduction. The midpoint potentials of the enzyme were determined by spectrotitration to be -0.294 V for disulfide/dithiol and -0.318 V for FAD/