Purification and characterization of cytochrome c(6) from Acaryochloris marina.
Cytochrome c(6), (cyt c(6)) a soluble monoheme electron transport protein, was isolated and characterized from the chlorophyll d-containing cyanobacterium Acaryochoris marina, the type strain MBIC11017. The protein was purified using ammonium sulfate precipitation, ion exchange and gel filtration column chromatography, and fast performance liquid chromatography. Its molecular mass and pI have been determined to be 8.87 kDa and less than 4.2, respectively, by mass spectrometry and isoelectrofocusing (IEF). The protein has an alpha helical structure as indicated by CD (circular dichroism) spectroscopy and a reduction midpoint potential (E(m)) of +327 mV versus the normal hydrogen electrode (NHE) as determined by redox potentiometry. Its potential role in electron transfer processes is discussed.
Bell
Patrick D
PD
Department of Chemistry, Washington University in St. Louis, St. Louis, MO 63130-4899, USA.
Xin
Yueyong
Y
Blankenship
Robert E
RE
D000595:Amino Acid Sequence; D002853:Chromatography, Liquid; D002942:Circular Dichroism; D000458:Cyanobacteria / Q000378:metabolism*; D045365:Cytochromes c6 / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D007525:Isoelectric Focusing; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013056:Spectrophotometry, Ultraviolet
D045365:Cytochromes c6
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