Respiratory system of Gluconacetobacter diazotrophicus PAL5 Evidence for a cyanide-sensitive cytochrome bb and cyanide-resistant cytochrome ba quinol oxidases

B. González, S. Martínez, J. L. Chávez, Sunhee Lee, N. A. Castro, M. A. Domínguez, S. Gómez, M. L. Contreras, C. Kennedy, J. E. Escamilla

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

In highly aerobic environments, Gluconacetobacter diazotrophicus uses a respiratory protection mechanism to preserve nitrogenase activity from deleterious oxygen. Here, the respiratory system was examined in order to ascertain the nature of the respiratory components, mainly of the cyanide sensitive and resistant pathways. The membranes of G. diazotrophicus contain Q 10 , Q 9 and PQQ in a 13:1:6.6 molar ratios. UV 360 nm photoinactivation indicated that ubiquinone is the electron acceptor for the dehydrogenases of the outer and inner faces of the membrane. Strong inhibition by rotenone and capsaicin and resistance to flavone indicated that NADH-quinone oxidoreductase is a NDH-1 type enzyme. KCN-titration revealed the presence of at least two terminal oxidases that were highly sensitive and resistant to the inhibitor. Tetrachorohydroquinol was preferentially oxidized by the KCN-sensitive oxidase. Neither the quinoprotein alcohol dehydrogenase nor its associated cytochromes c were instrumental components of the cyanide resistant pathway. CO-difference spectrum and photodissociation of heme-CO compounds suggested the presence of cytochromes b-CO and a 1 -CO adducts. Air-oxidation of cytochrome b (432 nm) was arrested by concentrations of KCN lower than 25 μM while cytochrome a 1 (442 nm) was not affected. A KCN-sensitive (I 50 = 5 μM) cytochrome bb and a KCN-resistant (I 50 = 450 μM) cytochrome ba quinol oxidases were separated by ion exchange chromatography.

Original languageEnglish (US)
Pages (from-to)1614-1622
Number of pages9
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1757
Issue number12
DOIs
StatePublished - Dec 1 2006
Externally publishedYes

Fingerprint

Gluconacetobacter
Respiratory system
Cyanides
Carbon Monoxide
Cytochromes
Respiratory System
Cytochromes a1
Oxidoreductases
flavone
Cytochromes b
Photodissociation
Membranes
Nitrogenase
Rotenone
Ubiquinone
Capsaicin
Ion Exchange Chromatography
Chromatography
Cytochromes c
Heme

Keywords

  • Acid acetic bacteria
  • Cyanide
  • Cytochrome quinol oxidase
  • Gluconacetobacter diazotrophicus
  • Respiratory chain

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

Cite this

Respiratory system of Gluconacetobacter diazotrophicus PAL5 Evidence for a cyanide-sensitive cytochrome bb and cyanide-resistant cytochrome ba quinol oxidases. / González, B.; Martínez, S.; Chávez, J. L.; Lee, Sunhee; Castro, N. A.; Domínguez, M. A.; Gómez, S.; Contreras, M. L.; Kennedy, C.; Escamilla, J. E.

In: Biochimica et Biophysica Acta - Bioenergetics, Vol. 1757, No. 12, 01.12.2006, p. 1614-1622.

Research output: Contribution to journalArticle

González, B. ; Martínez, S. ; Chávez, J. L. ; Lee, Sunhee ; Castro, N. A. ; Domínguez, M. A. ; Gómez, S. ; Contreras, M. L. ; Kennedy, C. ; Escamilla, J. E. / Respiratory system of Gluconacetobacter diazotrophicus PAL5 Evidence for a cyanide-sensitive cytochrome bb and cyanide-resistant cytochrome ba quinol oxidases. In: Biochimica et Biophysica Acta - Bioenergetics. 2006 ; Vol. 1757, No. 12. pp. 1614-1622.
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T1 - Respiratory system of Gluconacetobacter diazotrophicus PAL5 Evidence for a cyanide-sensitive cytochrome bb and cyanide-resistant cytochrome ba quinol oxidases

AU - González, B.

AU - Martínez, S.

AU - Chávez, J. L.

AU - Lee, Sunhee

AU - Castro, N. A.

AU - Domínguez, M. A.

AU - Gómez, S.

AU - Contreras, M. L.

AU - Kennedy, C.

AU - Escamilla, J. E.

PY - 2006/12/1

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N2 - In highly aerobic environments, Gluconacetobacter diazotrophicus uses a respiratory protection mechanism to preserve nitrogenase activity from deleterious oxygen. Here, the respiratory system was examined in order to ascertain the nature of the respiratory components, mainly of the cyanide sensitive and resistant pathways. The membranes of G. diazotrophicus contain Q 10 , Q 9 and PQQ in a 13:1:6.6 molar ratios. UV 360 nm photoinactivation indicated that ubiquinone is the electron acceptor for the dehydrogenases of the outer and inner faces of the membrane. Strong inhibition by rotenone and capsaicin and resistance to flavone indicated that NADH-quinone oxidoreductase is a NDH-1 type enzyme. KCN-titration revealed the presence of at least two terminal oxidases that were highly sensitive and resistant to the inhibitor. Tetrachorohydroquinol was preferentially oxidized by the KCN-sensitive oxidase. Neither the quinoprotein alcohol dehydrogenase nor its associated cytochromes c were instrumental components of the cyanide resistant pathway. CO-difference spectrum and photodissociation of heme-CO compounds suggested the presence of cytochromes b-CO and a 1 -CO adducts. Air-oxidation of cytochrome b (432 nm) was arrested by concentrations of KCN lower than 25 μM while cytochrome a 1 (442 nm) was not affected. A KCN-sensitive (I 50 = 5 μM) cytochrome bb and a KCN-resistant (I 50 = 450 μM) cytochrome ba quinol oxidases were separated by ion exchange chromatography.

AB - In highly aerobic environments, Gluconacetobacter diazotrophicus uses a respiratory protection mechanism to preserve nitrogenase activity from deleterious oxygen. Here, the respiratory system was examined in order to ascertain the nature of the respiratory components, mainly of the cyanide sensitive and resistant pathways. The membranes of G. diazotrophicus contain Q 10 , Q 9 and PQQ in a 13:1:6.6 molar ratios. UV 360 nm photoinactivation indicated that ubiquinone is the electron acceptor for the dehydrogenases of the outer and inner faces of the membrane. Strong inhibition by rotenone and capsaicin and resistance to flavone indicated that NADH-quinone oxidoreductase is a NDH-1 type enzyme. KCN-titration revealed the presence of at least two terminal oxidases that were highly sensitive and resistant to the inhibitor. Tetrachorohydroquinol was preferentially oxidized by the KCN-sensitive oxidase. Neither the quinoprotein alcohol dehydrogenase nor its associated cytochromes c were instrumental components of the cyanide resistant pathway. CO-difference spectrum and photodissociation of heme-CO compounds suggested the presence of cytochromes b-CO and a 1 -CO adducts. Air-oxidation of cytochrome b (432 nm) was arrested by concentrations of KCN lower than 25 μM while cytochrome a 1 (442 nm) was not affected. A KCN-sensitive (I 50 = 5 μM) cytochrome bb and a KCN-resistant (I 50 = 450 μM) cytochrome ba quinol oxidases were separated by ion exchange chromatography.

KW - Acid acetic bacteria

KW - Cyanide

KW - Cytochrome quinol oxidase

KW - Gluconacetobacter diazotrophicus

KW - Respiratory chain

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