Purification and characterization of membrane-bound CO-reactive hemoprotein from Tetrahymena pyriformis mitochondria.
A CO-reactive hemoprotein was purified from the mitochondrial membrane fraction of Tetrahymena pyriformis. It showed absorption peaks at 615 and 455 nm in the reduced form and an alpha peak at 565 nm in the pyridine ferrohemochrome spectrum. Although the spectral properties were apparently similar to those of 'cytochrome a620' which was previously proposed as a mitochondrial terminal oxidase in T. pyriformis, it did not contain any molecules of heme a or copper atoms. Further, it showed neither cytochrome c oxidase nor cytochrome c peroxidase activity. These results suggest that 'cytochrome a620' may not be the terminal oxidase in the mitochondrial respiratory chain of T. pyriformis.
Inokuchi
A
A
Department of Life Science, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
Fukumori
Y
Y
D000818:Animals; D002248:Carbon Monoxide / Q000378:metabolism*; D017936:Cytochrome a Group / Q000378:metabolism; D003576:Electron Transport Complex IV / Q000378:metabolism; D006420:Hemeproteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D007425:Intracellular Membranes / Q000378:metabolism; D007501:Iron / Q000032:analysis; D008928:Mitochondria / Q000378:metabolism; D015800:Protozoan Proteins; D013053:Spectrophotometry; D013769:Tetrahymena pyriformis / Q000378:metabolism*
D017936:Cytochrome a Group; D006420:Hemeproteins; D015800:Protozoan Proteins; C036213:cytochrome a620, Tetrahymena pytriformis; D002248:Carbon Monoxide; D007501:Iron; D003576:Electron Transport Complex IV