Spectral properties of Achromobacter xylosoxidans cytochromes c' and their NO complexes.
Cytochromes c' have been isolated from six strains of Achromobacter xylosoxidans: NCIB 11015 (formerly Alcaligenes sp. NCIB 11015), GIFU 543, 1048, 1051, 1055 and 1764. They are dimeric proteins with more positive redox potentials than those of cytochromes c' from phototrophic bacteria at neutral pH. The electronic absorption, EPR and MCD spectra on NO-ferrous cytochromes c' at physiological pH showed that the major part of the heme-iron of nitrosylheme was penta-coordinated. The EPR spectral results indicated that the ground state of the heme-iron of ferric cytochromes c' appears to be in an admixed spin states which consists of predominant high-spin with a slight intermediate-spin character at pH 7.2. These spectra were compared with those for cytochromes c' from phototrophic bacteria and the other hemoproteins.
Iwasaki
H
H
Nagoya University of Foreign Studies, Aichi, Japan.
Yoshimura
T
T
Suzuki
S
S
Shidara
S
S
D000421:Alcaligenes / Q000201:enzymology*; D001419:Bacteria / Q000201:enzymology; D003574:Cytochrome c Group / Q000737:chemistry* / Q000302:isolation & purification; D004578:Electron Spin Resonance Spectroscopy; D006418:Heme / Q000031:analogs & derivatives / Q000737:chemistry; D006420:Hemeproteins / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D009609:Nitrous Oxide / Q000737:chemistry*
D003574:Cytochrome c Group; D006420:Hemeproteins; D006418:Heme; C027417:nitrosylprotoheme; D009609:Nitrous Oxide