Cytochrome b from Escherichia coli nitrate reductase. Its properties and association with the enzyme complex.
作者： G R Chaudhry , C H MacGregor
DOI: 10.1016/S0021-9258(20)81967-X
关键词:
摘要: Membrane-bound nitrate reductase purified from Escherichia coli was resolved into two separate forms. The majority of the enzyme complex had a subunit composition 2A:2B:4C, exhibited cytochrome b spectra, and found to be stable after purification. A second form activity modified with 2A:2B lacked cytochrome. B this altered in its mobility on sodium dodecyl sulfate-polyacrylamide gels. cytochrome-containing 28 +/- 2 atoms iron 1.35 molybdenum whereas cytochromeless were 24 1.18 atoms/molecule, respectively. Besides reductase, other b-containing fractions also resolved. These associated formate dehydrogenase novel reduced absorption maxima at 430, 529.5, 560 nm. Nitrate (subunit C) isolated subunits as partially denatured renaturation accomplished by dialyzing against hemin. renatured yielded spectra similar holoenzyme. pure aggregated upon heating, even presence sulfate. It high isoelectric point (pH greater than 9.5) 45% hydrophobic amino acids.
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