Source:http://linkedlifedata.com/resource/pubmed/id/19266156
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2009-5-8
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pubmed:abstractText |
A membrane-anchored cytochrome c-550, which is highly expressed in obligately alkaliphilic Bacillus clarkii K24-1U, was purified and characterized. The protein contained a conspicuous sequence of Gly(22)-Asn(34), in comparison with the other Bacillus small cytochromes c. Analytical data indicated that the original and lipase-treated intermediate forms of cytochrome c-550 bind to fatty acids of C(15), C(16) and C(17) chain lengths and C(15) chain length, respectively, and it was considered that these fatty acids are bound to glycerol-Cys(18). Since there was a possibility that the presence of a diacylglycerol anchor contributed to the formation of dimeric states of this protein (20 and 17 kDa in SDS-PAGE), a C18M (Cys(18) --> Met)-cytochrome c-550 was constructed. The molecular mass of the C18M-cytochrome c-550 was determined as 15 and 10 kDa in SDS-PAGE and 23 kDa in blue native PAGE. The C18M-cytochrome c-550 bound with or without Triton X-100 formed a tetramer as the original cytochrome c-550 bound with Triton X-100, as determined by gel filtration. The midpoint redox potential of cytochrome c-550 as determined by redox titration was +83 mV, while that determined by cyclic voltammetric measurement was +7 mV. The above results indicate that cytochrome c-550 is a novel cytochrome c.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome c Group,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/cytochrome C-550
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1433-4909
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pubmed:author |
pubmed-author:HaraIsaoI,
pubmed-author:HijikataShoichiS,
pubmed-author:HoshinoTamotsuT,
pubmed-author:InoueNorioN,
pubmed-author:MatsunoToshihideT,
pubmed-author:MieYasuhiroY,
pubmed-author:MoritaNaokiN,
pubmed-author:OgamiShinichiS,
pubmed-author:TsukaharaTamotsuT,
pubmed-author:YamazakiKojiK,
pubmed-author:YokotaAtsushiA,
pubmed-author:YoshimuneKazuakiK,
pubmed-author:YumotoIsaoI
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pubmed:issnType |
Electronic
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pubmed:volume |
13
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
491-504
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pubmed:meshHeading |
pubmed-meshheading:19266156-Amino Acid Sequence,
pubmed-meshheading:19266156-Bacillus,
pubmed-meshheading:19266156-Base Sequence,
pubmed-meshheading:19266156-Chromatography, High Pressure Liquid,
pubmed-meshheading:19266156-Cytochrome c Group,
pubmed-meshheading:19266156-DNA Primers,
pubmed-meshheading:19266156-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:19266156-Fatty Acids,
pubmed-meshheading:19266156-Membrane Proteins,
pubmed-meshheading:19266156-Molecular Sequence Data,
pubmed-meshheading:19266156-Oxidation-Reduction,
pubmed-meshheading:19266156-Sequence Homology, Amino Acid,
pubmed-meshheading:19266156-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:19266156-Spectrophotometry, Ultraviolet
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pubmed:year |
2009
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pubmed:articleTitle |
A novel membrane-anchored cytochrome c-550 of alkaliphilic Bacillus clarkii K24-1U: expression, molecular features and properties of redox potential.
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pubmed:affiliation |
Research Institute of Genome-based Biofactory, National Institute of Advanced Industrial Science and Technology (AIST), Tsukisamu-Higashi, Toyohira-ku, Sapporo, 062-8517, Japan.
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pubmed:publicationType |
Journal Article
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