Purification and Characterization of Cytochrome O from Azotobacter Vinelandii

Overview

Journal Biochim Biophys Acta

Specialties Biochemistry
Biophysics

Date 1978 Jun 8

PMID 207321

Citations 4

Authors

T Y Yang

P JURTSHUK Jr

Affiliations

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Abstract

The membrane-bound cytochrome O has been solubilized from the Azotobacter vinelandii electron transport particle and further purified by use of conventional chromatographic procedures. The spectral characteristics as well as the other properties noted for purified cytochrome O are reported herein.

Citing Articles

Activation studies by phospholipids on the purified cytochrome c4:o oxidase of Azotobacter vinelandii.

Wong T, JURTSHUK Jr P J Bioenerg Biomembr. 1984; 16(5-6):477-89.

PMID: 6100376 DOI: 10.1007/BF00743240.

Isolation and characterization of TMPD-oxidase mutants of Pseudomonas aeruginosa.

Yang T Arch Microbiol. 1986; 144(3):228-32.

PMID: 3015066 DOI: 10.1007/BF00410952.

Immunological investigation of the distribution of cytochromes related to the two terminal oxidases of Escherichia coli in other gram-negative bacteria.

Kranz R, Gennis R J Bacteriol. 1985; 161(2):709-13.

PMID: 2981822 PMC: 214940. DOI: 10.1128/jb.161.2.709-713.1985.

The oxidation-reduction potentials of cytochrome o + c4 and cytochrome o purified from Azotobacter vinelandii.

Yang T, OKeefe D, Chance B Biochem J. 1979; 181(3):763-6.

PMID: 518554 PMC: 1161217. DOI: 10.1042/bj1810763.