NDLI: A High-Potential Soluble Cytochrome C -551 from the Purple Phototrophic Bacterium Chromatium vinosum is Homologous to Cytochrome C8 from Denitrifying Pseudomonads

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A High-Potential Soluble Cytochrome C -551 from the Purple Phototrophic Bacterium Chromatium vinosum is Homologous to Cytochrome C8 from Denitrifying Pseudomonads

Content Provider	Scilit
Author	Samyn, Bart Smet, Lina Driessche, Gonzalez Meyer, Terrance E. Bartsch, Robert G. Cusanovich, Michael A. Beeumen, Jozef J.
Copyright Year	1996
Description	Journal: Journal of Biological Inorganic Chemistry A minor cytochrome c-551 component of Chromatium vinosum was previously found to efficiently couple electron transfer between the cytochrome bc(1) complex and the photosynthetic reaction center. We have now determined the amino acid sequence of this cytochrome c-551 and find that it is homologous to cytochrome c(8) (formerly called Pseudomonas cytochrome c-551). It is most similar to Methylophilus methylotrophus, Rhodocyclus tenuis, and Azotobacter vinelandii cytochromes c(8) (respectively, 57%, 52% and 51%). The C. vinosum cytochrome c(8) has a single residue insertion relative to Pseudomonas and Azotobacter cytochromes c(8). It has fewer charged residues than its homologs and is essentially neutral, which may explain why it is less soluble than the others. The cytochromes c(8) are only very distantly related to the cytochromes c(2) found in other species of purple bacteria which are much larger in size and which usually mediate electron transfer between the cytochrome bc(1) complex and the reaction center. The photosynthetic pathway in Chromatium thus appears to be radically different from that in purple non-sulfur bacteria
Related Links	http://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1996.00689.x/pdf
Ending Page	696
Page Count	8
Starting Page	689
ISSN	09498257
e-ISSN	14321327
DOI	10.1111/j.1432-1033.1996.00689.x
Journal	Journal of Biological Inorganic Chemistry
Issue Number	2
Volume Number	236
Language	English
Publisher	Wiley-Blackwell
Publisher Date	1996-03-01
Access Restriction	Open
Subject Keyword	Journal: Journal of Biological Inorganic Chemistry Biochemistry and Molecular Biology Chromatium Vinosum Sequence Analysis Mass Spectrometry
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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Characterization of cytochrome c-556 from the purple phototrophic bacterium Rhodobacter capsulatus as a cytochrome-c peroxidase.

The amino acid sequence of cytochrome c' from the purple sulphur bacterium Chromatium vinosum.

Covalent structure of the flavoprotein subunit of the flavocytochrome c: sulfide dehydrogenase from the purple phototrophic bacterium Chromatium vinosum.

NOE and two-dimensional correlated 1H-NMR spectroscopy of cytochrome c' from Chromatium vinosum

1H and 13C NMR Assignments and Structural Aspects of a Ferrocytochrome c-551 from the Purple Phototrophic Bacterium Ectothiorhodospira halophila

Covalent structure of the flavoprotein subunit of the flavocytochrome c: sulfide dehydrogenase from the purple phototrophic bacterium Chromatium vinosum.

1H-NMR studies of high-potential iron-sulfur protein from the purple phototrophic bacterium, Rhodospirillum tenue

Nucleotide sequence of the heme subunit of flavocytochrome c from the purple phototrophic bacterium, Chromatium vinosum. A 2.6-kilobase pair DNA fragment contains two multiheme cytochromes, a flavoprotein, and a homolog of human ankyrin.

Nucleotide sequence of the heme subunit of flavocytochrome c from the purple phototrophic bacterium, Chromatium vinosum. A 2.6-kilobase pair DNA fragment contains two multiheme cytochromes, a flavoprotein, and a homolog of human ankyrin.

A High-Potential Soluble Cytochrome C -551 from the Purple Phototrophic Bacterium Chromatium vinosum is Homologous to Cytochrome C8 from Denitrifying Pseudomonads

Similar Documents

Characterization of cytochrome c-556 from the purple phototrophic bacterium Rhodobacter capsulatus as a cytochrome-c peroxidase.

The amino acid sequence of cytochrome c' from the purple sulphur bacterium Chromatium vinosum.

Covalent structure of the flavoprotein subunit of the flavocytochrome c: sulfide dehydrogenase from the purple phototrophic bacterium Chromatium vinosum.

NOE and two-dimensional correlated 1H-NMR spectroscopy of cytochrome c' from Chromatium vinosum

1H and 13C NMR Assignments and Structural Aspects of a Ferrocytochrome c-551 from the Purple Phototrophic Bacterium Ectothiorhodospira halophila

Covalent structure of the flavoprotein subunit of the flavocytochrome c: sulfide dehydrogenase from the purple phototrophic bacterium Chromatium vinosum.

1H-NMR studies of high-potential iron-sulfur protein from the purple phototrophic bacterium, Rhodospirillum tenue

Nucleotide sequence of the heme subunit of flavocytochrome c from the purple phototrophic bacterium, Chromatium vinosum. A 2.6-kilobase pair DNA fragment contains two multiheme cytochromes, a flavoprotein, and a homolog of human ankyrin.

Nucleotide sequence of the heme subunit of flavocytochrome c from the purple phototrophic bacterium, Chromatium vinosum. A 2.6-kilobase pair DNA fragment contains two multiheme cytochromes, a flavoprotein, and a homolog of human ankyrin.

A High-Potential Soluble Cytochrome C -551 from the Purple Phototrophic Bacterium Chromatium vinosum is Homologous to Cytochrome C8 from Denitrifying Pseudomonads