• We are sorry, but NCBI web applications do not support your browser and may not function properly. More information
Logo of jbacterPermissionsJournals.ASM.orgJournalJB ArticleJournal InfoAuthorsReviewers
J Bacteriol. Apr 1992; 174(7): 2338–2343.
PMCID: PMC205856

Spectroscopic and genetic evidence for two heme-Cu-containing oxidases in Rhodobacter sphaeroides.

Abstract

It has recently become evident that many bacterial respiratory oxidases are members of a superfamily that is related to the eukaryotic cytochrome c oxidase. These oxidases catalyze the reduction of oxygen to water at a heme-copper binuclear center. Fourier transform infrared (FTIR) spectroscopy has been used to examine the heme-copper-containing respiratory oxidases of Rhodobacter sphaeroides Ga. This technique monitors the stretching frequency of CO bound at the oxygen binding site and can be used to characterize the oxidases in situ with membrane preparations. Oxidases that have a heme-copper binuclear center are recognizable by FTIR spectroscopy because the bound CO moves from the heme iron to the nearby copper upon photolysis at low temperature, where it exhibits a diagnostic spectrum. The FTIR spectra indicate that the binuclear center of the R. sphaeroides aa3-type cytochrome c oxidase is remarkably similar to that of the bovine mitochondrial oxidase. Upon deletion of the ctaD gene, encoding subunit I of the aa3-type oxidase, substantial cytochrome c oxidase remains in the membranes of aerobically grown R. sphaeroides. This correlates with a second wild-type R. sphaeroides is grown photosynthetically, the chromatophore membranes lack the aa3-type oxidase but have this second heme-copper oxidase. Subunit I of the heme-copper oxidase superfamily contains the binuclear center. Amino acid sequence alignments show that this subunit is structurally very highly conserved among both eukaryotic and prokaryotic species. The polymerase chain reaction was used to show that the chromosome of R. sphaeroides contains at least one other gene that is a homolog of ctaD, the gene encoding subunit I of the aa3-type cytochrome c oxidase.(ABSTRACT TRUNCATED AT 250 WORDS)

Full text

Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (1.1M), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References.

Images in this article

Click on the image to see a larger version.

Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Cao J, Shapleigh J, Gennis R, Revzin A, Ferguson-Miller S. The gene encoding cytochrome c oxidase subunit II from Rhodobacter sphaeroides; comparison of the deduced amino acid sequence with sequences of corresponding peptides from other species. Gene. 1991 May 15;101(1):133–137. [PubMed]
  • Capaldi RA. Structure and assembly of cytochrome c oxidase. Arch Biochem Biophys. 1990 Aug 1;280(2):252–262. [PubMed]
  • Capaldi RA. Structure and function of cytochrome c oxidase. Annu Rev Biochem. 1990;59:569–596. [PubMed]
  • Chan SI, Li PM. Cytochrome c oxidase: understanding nature's design of a proton pump. Biochemistry. 1990 Jan 9;29(1):1–12. [PubMed]
  • Chepuri V, Lemieux L, Au DC, Gennis RB. The sequence of the cyo operon indicates substantial structural similarities between the cytochrome o ubiquinol oxidase of Escherichia coli and the aa3-type family of cytochrome c oxidases. J Biol Chem. 1990 Jul 5;265(19):11185–11192. [PubMed]
  • Chepuri V, Lemieux L, Hill J, Alben JO, Gennis RB. Recent studies of the cytochrome o terminal oxidase complex of Escherichia coli. Biochim Biophys Acta. 1990 Jul 25;1018(2-3):124–127. [PubMed]
  • COHEN-BAZIRE G, SISTROM WR, STANIER RY. Kinetic studies of pigment synthesis by non-sulfur purple bacteria. J Cell Physiol. 1957 Feb;49(1):25–68. [PubMed]
  • Einarsdóttir O, Killough PM, Fee JA, Woodruff WH. An infrared study of the binding and photodissociation of carbon monoxide in cytochrome ba3 from Thermus thermophilus. J Biol Chem. 1989 Feb 15;264(5):2405–2408. [PubMed]
  • Fiamingo FG, Alben JO. Structures of photolyzed carboxymyoglobin. Biochemistry. 1985 Dec 31;24(27):7964–7970. [PubMed]
  • Fiamingo FG, Altschuld RA, Moh PP, Alben JO. Dynamic interactions of CO with a3Fe and CuB in cytochrome c oxidase in beef heart mitochondria studied by Fourier transform infrared spectroscopy at low temperatures. J Biol Chem. 1982 Feb 25;257(4):1639–1650. [PubMed]
  • Fiamingo FG, Jung DW, Alben JO. Structural perturbation of the a3-CuB site in mitochondrial cytochrome c oxidase by alcohol solvents. Biochemistry. 1990 May 15;29(19):4627–4633. [PubMed]
  • Garcia-Horsman JA, Barquera B, Escamilla JE. Two different aa3-type cytochromes can be purified from the bacterium Bacillus cereus. Eur J Biochem. 1991 Aug 1;199(3):761–768. [PubMed]
  • Gennis RB. Some recent advances relating to prokaryotic cytochrome c reductases and cytochrome c oxidases. Biochim Biophys Acta. 1991 May 23;1058(1):21–24. [PubMed]
  • Puustinen A, Wikström M. The heme groups of cytochrome o from Escherichia coli. Proc Natl Acad Sci U S A. 1991 Jul 15;88(14):6122–6126. [PMC free article] [PubMed]
  • Raitio M, Pispa JM, Metso T, Saraste M. Are there isoenzymes of cytochrome c oxidase in Paracoccus denitrificans? FEBS Lett. 1990 Feb 26;261(2):431–435. [PubMed]
  • Sanger F, Nicklen S, Coulson AR. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. [PMC free article] [PubMed]
  • Saraste M. Structural features of cytochrome oxidase. Q Rev Biophys. 1990 Nov;23(4):331–366. [PubMed]
  • Sasaki T, Motokawa Y, Kikuchi G. Occurrence of both a-type and o-type cytochromes as the functional terminal oxidases in Rhodopseudomonas spheroides. Biochim Biophys Acta. 1970 Mar 3;197(2):284–291. [PubMed]
  • Sone N, Kutoh E, Sato K. A cytochrome o-type oxidase of the thermophilic bacterium PS3 grown under air-limited conditions. J Biochem. 1990 Apr;107(4):597–602. [PubMed]
  • van der Oost J, von Wachenfeld C, Hederstedt L, Saraste M. Bacillus subtilis cytochrome oxidase mutants: biochemical analysis and genetic evidence for two aa3-type oxidases. Mol Microbiol. 1991 Aug;5(8):2063–2072. [PubMed]
  • Woese CR. Bacterial evolution. Microbiol Rev. 1987 Jun;51(2):221–271. [PMC free article] [PubMed]
  • Yang D, Oyaizu Y, Oyaizu H, Olsen GJ, Woese CR. Mitochondrial origins. Proc Natl Acad Sci U S A. 1985 Jul;82(13):4443–4447. [PMC free article] [PubMed]
  • Yoshikawa S, Caughey WS. Infrared evidence of cyanide binding to iron and copper sites in bovine heart cytochrome c oxidase. Implications regarding oxygen reduction. J Biol Chem. 1990 May 15;265(14):7945–7958. [PubMed]
  • Yun CH, Beci R, Crofts AR, Kaplan S, Gennis RB. Cloning and DNA sequencing of the fbc operon encoding the cytochrome bc1 complex from Rhodobacter sphaeroides. Characterization of fbc deletion mutants and complementation by a site-specific mutational variant. Eur J Biochem. 1990 Dec 12;194(2):399–411. [PubMed]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

Formats:

Related citations in PubMed

See reviews...See all...

Cited by other articles in PMC

See all...

Links

Recent Activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...