The cytochromebdterminal oxidase ofAzotobacter vinelandii: Low temperature photodissociation spectrophotometry reveals reactivity of cytochromesb595anddwith both carbon monoxide and oxygen

Author:

D'mello Rita,Palmer Sarah,Hill Susan,Poole Robert K.

Publisher

Oxford University Press (OUP)

Subject

Genetics,Molecular Biology,Microbiology

Reference18 articles.

1. Bacteriol cytochrome oxidases: a structurally and functionally diverse group of electron transfer proteins;Poole;Biochim. Biophys. Acta,1983

2. 2 Hill, J.J. , Alben, J.O. and Gennis, R.B. (1993) Spectroscopic evidence for a heme-heme binuclear centre in the cytochrome bd ubiquinol oxidase from Escherichia coli 2nd edn., 90, In Proc. Natl. Acad. Sci. USA, pp 5863–5867.

3. The 650 nm chromophore in Escherichia coli is an “oxy” - or oxygenated compound, not the oxidized form of cytochrome oxidase d: a hypothesis;Poole;J. Gen. Microbiol.,1983

4. Resonance Raman spectroscopy of an oxygenated intermediate species of cytochrome oxidase d from Escherichia coli;Poole;FEBS Lett.,1982

5. Spectroscopic and quantitative analysis of the oxygenated and peroxy states of the purified cytochrome d complex of Escherichia coli;Lorence;J. Biol. Chem.,1989

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