Spectral Properties of Cytochrome c553 and a Membrane-Bound Cytochrome b from Alcaligenes xylosoxidans GIFU 1051.
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Cytochrome c553 and cytochrome b were isolated from soluble and membrane fractions of Alcaligenes xylosoxidans GIFU 1051, respectively, and their spectroscopic characterizations have been performed. Cytochrome c553 has been shown to be in the low spin state both in the oxidized and reduced forms at room temperature by the absorption and magnetic circular dichroism (MCD) spectra, while the high spin heme has been also observed in the cryogenic electron paramagnetic resonance (EPR) spectra. Exogenous small ligands such as NO and CO bind to cytochrome c553 by expelling the axial His ligand. The membrane-bound cytochrome b has two heme b centers in a protein molecule which are the active centers of NO reductase, the cytochrome bc complex, although the enzyme activity was rather low. The absorption, MCD, and EPR spectra of the membrane-bound cytochrome b showed that two heme b centers are in the different electronic states, the high and low spin states. Cytochrome c553 is the natural electron donor to the membrane-bound NO reductase, although the interprotein electron-transfer could not been studied because of the low enzyme activity of the cytochrome b subunit.
- 公益社団法人 日本化学会の論文
公益社団法人 日本化学会 | 論文
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