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The primary structure of cytochrome c-554 from the green photosynthetic bacterium Chloroflexus aurantiacus
The complete nucleotide sequence of the cytochrome c-554 gene from the green photosynthetic bacterium Chloroflexus aurantiacus has been determined. The derived amino acid sequence showed that the cytochrome precursor protein consists of 414 residues and contains 4-Cys-X-X-Cys-His- heme binding motif...
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Published in: | Biochemistry (Easton) 1991-12, Vol.30 (48), p.11451-11458 |
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creator | Dracheva, Stella Williams, JoAnn C Van Driessche, Gonzalez Van Beeumen, Jozef J Blankenship, Robert E |
description | The complete nucleotide sequence of the cytochrome c-554 gene from the green photosynthetic bacterium Chloroflexus aurantiacus has been determined. The derived amino acid sequence showed that the cytochrome precursor protein consists of 414 residues and contains 4-Cys-X-X-Cys-His- heme binding motifs. The only regions of the cytochrome c-554 sequence that were found to be significantly similar to the sequences of cytochromes from other organisms were the heme binding sites. The highest similarity was found with the heme binding segments in the four-heme reaction center cytochrome subunit from the purple photosynthetic bacterium Rhodopseudomonas viridis. The importance of this similarity for the evolutionary relationship between Chloroflexus and the purple bacteria is discussed. |
doi_str_mv | 10.1021/bi00112a012 |
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The derived amino acid sequence showed that the cytochrome precursor protein consists of 414 residues and contains 4-Cys-X-X-Cys-His- heme binding motifs. The only regions of the cytochrome c-554 sequence that were found to be significantly similar to the sequences of cytochromes from other organisms were the heme binding sites. The highest similarity was found with the heme binding segments in the four-heme reaction center cytochrome subunit from the purple photosynthetic bacterium Rhodopseudomonas viridis. The importance of this similarity for the evolutionary relationship between Chloroflexus and the purple bacteria is discussed.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00112a012</identifier><identifier>PMID: 1660302</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>140505 - Solar Energy Conversion- Photochemical, Photobiological, & Thermochemical Conversion- (1980-) ; AMINO ACID SEQUENCE ; Base Sequence ; Binding Sites ; Biological and medical sciences ; BIOLOGICAL EVOLUTION ; Blotting, Southern ; CARBOXYLIC ACIDS ; Chlorophyta - chemistry ; Cloning, Molecular ; Codon ; Cytochrome c Group - chemistry ; Cytochrome c Group - genetics ; Cytochrome c Group - metabolism ; cytochrome c554 ; CYTOCHROMES ; DNA - chemistry ; DNA - genetics ; DNA SEQUENCING ; Fundamental and applied biological sciences. Psychology ; GENES ; Genes. 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The derived amino acid sequence showed that the cytochrome precursor protein consists of 414 residues and contains 4-Cys-X-X-Cys-His- heme binding motifs. The only regions of the cytochrome c-554 sequence that were found to be significantly similar to the sequences of cytochromes from other organisms were the heme binding sites. The highest similarity was found with the heme binding segments in the four-heme reaction center cytochrome subunit from the purple photosynthetic bacterium Rhodopseudomonas viridis. The importance of this similarity for the evolutionary relationship between Chloroflexus and the purple bacteria is discussed.</description><subject>140505 - Solar Energy Conversion- Photochemical, Photobiological, & Thermochemical Conversion- (1980-)</subject><subject>AMINO ACID SEQUENCE</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>BIOLOGICAL EVOLUTION</subject><subject>Blotting, Southern</subject><subject>CARBOXYLIC ACIDS</subject><subject>Chlorophyta - chemistry</subject><subject>Cloning, Molecular</subject><subject>Codon</subject><subject>Cytochrome c Group - chemistry</subject><subject>Cytochrome c Group - genetics</subject><subject>Cytochrome c Group - metabolism</subject><subject>cytochrome c554</subject><subject>CYTOCHROMES</subject><subject>DNA - chemistry</subject><subject>DNA - genetics</subject><subject>DNA SEQUENCING</subject><subject>Fundamental and applied biological sciences. 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Psychology</topic><topic>GENES</topic><topic>Genes. Genome</topic><topic>HEME</topic><topic>Heme - metabolism</topic><topic>HETEROCYCLIC ACIDS</topic><topic>HETEROCYCLIC COMPOUNDS</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>MOLECULAR STRUCTURE</topic><topic>Molecular Weight</topic><topic>ORGANIC ACIDS</topic><topic>ORGANIC COMPOUNDS</topic><topic>ORGANIC NITROGEN COMPOUNDS</topic><topic>PHOTOSYNTHETIC BACTERIA</topic><topic>PIGMENTS</topic><topic>Polymerase Chain Reaction</topic><topic>PORPHYRINS</topic><topic>PROTEINS</topic><topic>Restriction Mapping</topic><topic>SOLAR ENERGY</topic><topic>Space life sciences</topic><topic>STRUCTURAL CHEMICAL ANALYSIS</topic><topic>THERMOPHILIC CONDITIONS</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dracheva, Stella</creatorcontrib><creatorcontrib>Williams, JoAnn C</creatorcontrib><creatorcontrib>Van Driessche, Gonzalez</creatorcontrib><creatorcontrib>Van Beeumen, Jozef J</creatorcontrib><creatorcontrib>Blankenship, Robert E</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dracheva, Stella</au><au>Williams, JoAnn C</au><au>Van Driessche, Gonzalez</au><au>Van Beeumen, Jozef J</au><au>Blankenship, Robert E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The primary structure of cytochrome c-554 from the green photosynthetic bacterium Chloroflexus aurantiacus</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1991-12-01</date><risdate>1991</risdate><volume>30</volume><issue>48</issue><spage>11451</spage><epage>11458</epage><pages>11451-11458</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>The complete nucleotide sequence of the cytochrome c-554 gene from the green photosynthetic bacterium Chloroflexus aurantiacus has been determined. The derived amino acid sequence showed that the cytochrome precursor protein consists of 414 residues and contains 4-Cys-X-X-Cys-His- heme binding motifs. The only regions of the cytochrome c-554 sequence that were found to be significantly similar to the sequences of cytochromes from other organisms were the heme binding sites. The highest similarity was found with the heme binding segments in the four-heme reaction center cytochrome subunit from the purple photosynthetic bacterium Rhodopseudomonas viridis. The importance of this similarity for the evolutionary relationship between Chloroflexus and the purple bacteria is discussed.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>1660302</pmid><doi>10.1021/bi00112a012</doi><tpages>8</tpages></addata></record> |
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subjects | 140505 - Solar Energy Conversion- Photochemical, Photobiological, & Thermochemical Conversion- (1980-) AMINO ACID SEQUENCE Base Sequence Binding Sites Biological and medical sciences BIOLOGICAL EVOLUTION Blotting, Southern CARBOXYLIC ACIDS Chlorophyta - chemistry Cloning, Molecular Codon Cytochrome c Group - chemistry Cytochrome c Group - genetics Cytochrome c Group - metabolism cytochrome c554 CYTOCHROMES DNA - chemistry DNA - genetics DNA SEQUENCING Fundamental and applied biological sciences. Psychology GENES Genes. Genome HEME Heme - metabolism HETEROCYCLIC ACIDS HETEROCYCLIC COMPOUNDS Molecular and cellular biology Molecular genetics Molecular Sequence Data MOLECULAR STRUCTURE Molecular Weight ORGANIC ACIDS ORGANIC COMPOUNDS ORGANIC NITROGEN COMPOUNDS PHOTOSYNTHETIC BACTERIA PIGMENTS Polymerase Chain Reaction PORPHYRINS PROTEINS Restriction Mapping SOLAR ENERGY Space life sciences STRUCTURAL CHEMICAL ANALYSIS THERMOPHILIC CONDITIONS |
title | The primary structure of cytochrome c-554 from the green photosynthetic bacterium Chloroflexus aurantiacus |
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