CYTOCHROMES C-552 FROM 2 STRAINS OF THE HYDROGENOTROPHIC BACTERIUM ALCALIGENES-EUTROPHUS ARE SEQUENCE HOMOLOGS OF THE CYTOCHROMES C(8) FROMTHE DENITRIFYING PSEUDOMONADS
K. Klarskov et al., CYTOCHROMES C-552 FROM 2 STRAINS OF THE HYDROGENOTROPHIC BACTERIUM ALCALIGENES-EUTROPHUS ARE SEQUENCE HOMOLOGS OF THE CYTOCHROMES C(8) FROMTHE DENITRIFYING PSEUDOMONADS, Biochimica et biophysica acta. Protein structure and molecular enzymology, 1343(2), 1997, pp. 144-151
Soluble cytochromes c-552 were purified from two strains of the hydrog
enothrophic species Alcaligenes eutrophus and their amino acid sequenc
es determined. The two cytochromes were found to have 5 differences ou
t of a total of 89 residues. The proteins are clearly related to the c
ytochromes c(8) (formerly called Pseudomonas cytochromes c-551), but r
equire a single residue insertion after the methionine sixth heme liga
nd relative to the Pseudomonas aeruginosa protein. The consensus resid
ues Trp56 and Trp77. characteristic for the c(8) family, are also pres
ent in the Alcaligenes proteins. Overall, the Alcaligenes cytochromes
are only 43% identical to the Pseudomonas proteins which average 68% i
dentity to one another. They are also only 45% identical to cytochrome
c(8) from Hydrogenobacter thermophilus, another hydrogenothrophic spe
cies, which indicates that the hydrogen utilizing bacteria are not mor
e closely related to one another than they are to other species. The f
inding of cytochrome c(8) in Alcaligenes eutrophus completes the recen
t characterization of a cytochrome cd(1)-nitrite reductase from this b
acterial species and suggests the existence of the same denitrificatio
n pathway as in Pseudomonas where these two proteins are reaction part
ners. (C) 1997 Elsevier Science B.V.