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Biochim Biophys Acta. 1985 Jan 23;806(1):175-83.

Isolation and characterization of soluble cytochromes, ferredoxins and other chromophoric proteins from the halophilic phototrophic bacterium Ectothiorhodospira halophila.

Abstract

A cytochrome c-551 and a pair of 'high redox-potential' ferredoxins (iso-high-potential iron-sulfur proteins) were found to be the major soluble electron-transport proteins in Ectothiorhodospira halophila. Smaller amounts of 'bacterial' ferredoxin and cytochrome c' were also observed. With the exception of cytochrome c-551, these proteins are commonly encountered in the purple sulfur bacteria, family Chromatiaceae and less frequently in the purple bacteria, family Rhodospirillaceae. In addition to the cytochromes and ferredoxins, E. halophila synthesizes substantial amounts of a small yellow-colored protein, which has a chromophore spectrally similar to flavins having oxygen, nitrogen or sulfur substituents in place of the 8-methyl group such as roseoflavin and the methanogen cofactor F-420. A purple-colored protein was only partially purified, but it is spectrally similar to iron proteins having a tyrosine ligand, such as transferrin, catechuate dioxygenase, and especially the purple acid phosphatases. Neither the yellow protein nor the purple one has previously been observed in phototrophic bacteria, but may in some way be required for survival in extremely halophilic habitats. The only feature common to halophiles including E. halophila is the very acidic nature of their proteins.

PMID:
2981543
DOI:
10.1016/0005-2728(85)90094-5
[Indexed for MEDLINE]

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