Purification and some properties of cytochrome c' from a strain of Achromobacter xylosoxidans.
Cytochrome c' was crystallized from Achromobacter xylosoxidans GIFU 543. The cytochrome was a basic protein and its molecular weight was 28,000. The pyridine ferrohemochrome showed absorption peaks at 415, 521, and 551 nm. The absorption spectra of the oxidized and reduced forms at neutral pH were almost the same as those of other cytochromes c' reported already. The reduced cytochrome c' reacted with CO and NO, and the NO complex showed a characteristic absorption spectrum. The midpoint redox potential of the hemoprotein was measured to be + 110 mV at pH 7.2.
D000421:Alcaligenes / Q000201:enzymology*; D003460:Crystallization; D003574:Cytochrome c Group / Q000302:isolation & purification*; D007526:Isoelectric Point; D008970:Molecular Weight; D010084:Oxidation-Reduction; D013053:Spectrophotometry
D003574:Cytochrome c Group