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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Bibliographic Details
Published in:Biochemistry (Easton) 1991-12, Vol.30 (48), p.11451-11458
Main Authors: Dracheva, Stella, Williams, JoAnn C, Van Driessche, Gonzalez, Van Beeumen, Jozef J, Blankenship, Robert E
Format: Article
Language:English
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
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Summary: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.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00112a012