The bc1 complex of the iron-grown acidophilic chemolithotrophic bacterium Acidithiobacillus ferrooxidans functions in the reverse but not in the forward direction.: Is there a second bc1 complex?

被引:51
作者
Brasseur, G
Bruscella, P
Bonnefoy, V
Lemesle-Meunier, D
机构
[1] CNRS, Lab Bioenerget & Ingn Prot, Inst Biol Struct & Microbiol, F-13402 Marseille 20, France
[2] CNRS, Chim Bacterienne Lab, Inst Biol Struct & Microbiol, F-13402 Marseille 20, France
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 2002年 / 1555卷 / 1-3期
关键词
Acidithiobacillus ferrooxidans; bc(1) complex; reverse electron transfer; cytochrome b; Rieske protein; acidophilic chemolithotrophic bacteria;
D O I
10.1016/S0005-2728(02)00251-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Acidithiobacillus ferrooxidans is an acidophilic chemolithotrophic bacterium that can grow in the presence of either a weak reductant, Fe2+, or reducing sulfur compounds that provide more energy for growth than Fe. Here we first review the latest findings about the uphill electron transfer pathway established in iron-grown A. ferrooxidans, which has been found to involve a bc(1) complex. We then provide evidence that this bc(1) complex cannot function in the forward direction (exergonic reaction), even with an appropriate substrate. A search for the sequence of the three redox subunits of the A. ferrooxidans bc(1) complex (strain ATCC 19859) in the complete genome sequence of the A. ferrooxidans ATCC 23270 strain showed the existence of two different bc(1) complexes in A. ferrooxidans. Cytochrome b and Rieske protein sequence comparisons allowed us to point out some sequence particularities of these proteins in A. ferrooxidans. Lastly, we discuss the possible reasons for the existence of two different "classical" bc(1) complexes and put forward some suggestions as to what role these putative complexes may play in this acidophilic chemolithotrophic bacterium. (C) 2002 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:37 / 43
页数:7
相关论文
共 34 条
  • [1] Appia-Ayme C, 1999, APPL ENVIRON MICROB, V65, P4781
  • [2] Structure and function of cytochrome bc complexes
    Berry, EA
    Guergova-Kuras, M
    Huang, LS
    Crofts, AR
    [J]. ANNUAL REVIEW OF BIOCHEMISTRY, 2000, 69 : 1005 - 1075
  • [3] RESPIRATORY ENZYMES OF THIOBACILLUS-FERROOXIDANS - KINETIC-PROPERTIES OF AN ACID-STABLE IRON-RUSTICYANIN OXIDOREDUCTASE
    BLAKE, RC
    SHUTE, EA
    [J]. BIOCHEMISTRY, 1994, 33 (31) : 9220 - 9228
  • [4] Diversity of cytochrome bc complexes:: Example of the Rieske protein in green sulfur bacteria
    Brugna, M
    Albouy, D
    Nitschke, W
    [J]. JOURNAL OF BACTERIOLOGY, 1998, 180 (14) : 3719 - 3723
  • [5] Redox components of cytochrome bc-type enzymes in acidophilic prokaryotes II.: The Rieske protein of phylogenetically distant acidophilic organisms
    Brugna, M
    Nitschke, W
    Asso, M
    Guigliarelli, B
    Lemesle-Meunier, D
    Schmidt, C
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (24) : 16766 - 16772
  • [6] CAVAZZA C, 1995, FEMS MICROBIOL LETT, V130, P193
  • [7] Characterisation of a soluble cytochrome c(4) isolated from Thiobacillus ferrooxidans
    Cavazza, C
    GiudiciOrticoni, MT
    Nitschke, W
    Appia, C
    Bonnefoy, V
    Bruschi, M
    [J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 1996, 242 (02): : 308 - 314
  • [8] RESPIRATORY-CHAIN OF THIOBACILLUS-FERROOXIDANS - REDUCTION OF CYTOCHROMES BY FE2+ AND PRELIMINARY CHARACTERIZATION OF RUSTICYANIN A NOVEL BLUE COPPER PROTEIN
    COBLEY, JG
    HADDOCK, BA
    [J]. FEBS LETTERS, 1975, 60 (01): : 29 - 33
  • [9] CORBETT CM, 1987, FEMS MICROBIOL LETT, V41, P1
  • [10] PURIFICATION AND SOME PROPERTIES OF RUSTICYANIN, A BLUE COPPER PROTEIN INVOLVED IN IRON(II) OXIDATION FROM THIOBACILLUS-FERROOXIDANS
    COX, JC
    BOXER, DH
    [J]. BIOCHEMICAL JOURNAL, 1978, 174 (02) : 497 - 502