title: Purification and characterization of cytochrome c(6) from Acaryochloris marina.
abstract: 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.
authors.affiliation: Department of Chemistry, Washington University in St. Louis, St. Louis, MO 63130-4899, USA.
authors.forename: Patrick D
authors.initials: PD
authors.lastname: Bell
authors.forename: Yueyong
authors.initials: Y
authors.lastname: Xin
authors.forename: Robert E
authors.initials: RE
authors.lastname: Blankenship
mesh_terms: 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
chemical_list: D045365:Cytochromes c6
references.citation: J Biol Chem. 1999 May 7;274(19):13292-7
references.pmid: 10224089
references.citation: Proc Natl Acad Sci U S A. 1998 Oct 27;95(22):13319-23
references.pmid: 9789086
references.citation: FEBS Lett. 2005 Apr 25;579(11):2273-6
references.pmid: 15848157
references.citation: J Phys Chem B. 2008 Jun 26;112(25):7351-4
references.pmid: 18512893
references.citation: J Am Chem Soc. 2007 Aug 1;129(30):9468-75
references.pmid: 17625855
references.citation: Proc Natl Acad Sci U S A. 2009 Apr 14;106(15):6134-9
references.pmid: 19339500
references.citation: J Biol Chem. 2008 Jun 27;283(26):18198-209
references.pmid: 18458090
references.citation: Proc Natl Acad Sci U S A. 2008 Feb 12;105(6):2005-10
references.pmid: 18252824
references.citation: Eur J Biochem. 2000 Jul;267(13):4232-41
references.pmid: 10866828
references.citation: J Biol Chem. 2008 Sep 12;283(37):25218-25226
references.pmid: 18635535
references.citation: J Am Chem Soc. 2003 Nov 12;125(45):13686-92
references.pmid: 14599207
references.citation: Photosynth Res. 2008 Oct-Dec;98(1-3):141-9
references.pmid: 18985431
references.citation: Eur J Biochem. 1993 May 1;213(3):1133-8
references.pmid: 8504808
references.citation: J Am Chem Soc. 2006 Feb 8;128(5):1580-6
references.pmid: 16448129
references.citation: Proc Natl Acad Sci U S A. 2005 Jan 18;102(3):850-5
references.pmid: 15637160
references.citation: Plant Cell Physiol. 2007 Jul;48(7):948-57
references.pmid: 17548374
references.citation: Photosynth Res. 2003;75(2):97-110
references.pmid: 16245081
references.citation: Appl Environ Microbiol. 2005 Dec;71(12):8606-10
references.pmid: 16332853
references.citation: Annu Rev Plant Physiol Plant Mol Biol. 1998 Jun;49:397-425
references.pmid: 15012240
references.citation: Eur J Biochem. 1993 Aug 15;216(1):329-41
references.pmid: 8396033
references.citation: Biochim Biophys Acta. 1999 Oct 6;1413(2):92-7
references.pmid: 10514550
references.citation: Methods Enzymol. 1978;54:411-35
references.pmid: 732578
references.citation: Biochemistry. 2008 May 20;47(20):5515-22
references.pmid: 18439023
references.citation: Photosynth Res. 2008 Oct-Dec;98(1-3):131-40
references.pmid: 18839331
references.citation: J Mol Biol. 2006 Jul 28;360(5):968-77
references.pmid: 16815443