The cellular location and specificity of bacterial cytochrome c peroxidases.
The locations of cytochrome c peroxidase and catalase activities in the two Gram-negative bacteria Pseudomonas stutzeri (N.C.I.B. 9721) and Paracoccus denitrificans (N.C.I.B. 8944) were investigated by the production of spheroplasts. In both species the cytochrome c peroxidase was predominantly periplasmic: 92% of total activity in Ps. stutzeri and 98% of nonmembrane-bound activity in Pa. denitrificans were found in this cellular compartment. In contrast, the catalase was mostly in the cytoplasmic fraction. Purification of the Pa. denitrificans cytochrome c peroxidase showed it to be the haem c-containing polypeptide of Mr 42,000 that has already been described by Bosma, Braster, Stouthamer & Van Versefeld [(1987) Eur. J. Biochem. 165, 665-670] but was not identified by them as a peroxidase. The visible-absorption spectra of the enzyme closely resemble those of cytochrome c peroxidase from Pseudomonas aeruginosa but the donor specificity is different, with the Pa. denitrificans enzyme preferring the basic mitochondrial cytochromes c to the acidic cytochromes c-551 and reacting well with the Pa. denitrificans cytochrome c-550.
Goodhew
C F
CF
Department of Preclinical Veterinary Sciences, University of Edinburgh, U.K.
Wilson
I B
IB
Hunter
D J
DJ
Pettigrew
G W
GW
D001426:Bacterial Proteins / Q000302:isolation & purification / Q000378:metabolism*; D002374:Catalase / Q000378:metabolism; D003574:Cytochrome c Group / Q000378:metabolism; D003578:Cytochrome-c Peroxidase / Q000302:isolation & purification / Q000378:metabolism*; D010231:Paracoccus denitrificans / Q000201:enzymology; D011549:Pseudomonas / Q000201:enzymology; D011550:Pseudomonas aeruginosa / Q000201:enzymology; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D013104:Spheroplasts / Q000201:enzymology
D001426:Bacterial Proteins; D003574:Cytochrome c Group; C017167:cytochrome C(551); C031732:cytochrome C-550; D003578:Cytochrome-c Peroxidase; D002374:Catalase