Electron Transport Systems for Quinohemoprotein Type II Alcohol Dehydrogenase of Pseudomonas Putida HK5

2000 ◽  
pp. 219-224 ◽  
Author(s):  
Kazunobu Matsushita ◽  
Tetsuo Yamashita ◽  
Nahoko Aoki ◽  
Hirohide Toyama ◽  
Osao Adachi
Keyword(s):  
Electron Transport ◽  
Alcohol Dehydrogenase ◽  
Pseudomonas Putida ◽  
Transport Systems ◽  
Type Ii

Comparative studies on succinate and terminal oxidase activity in microbial and mammalian electron-transport systems

1969 ◽  
Vol 15 (7) ◽  
pp. 797-807 ◽  
Author(s):  
Peter Jurtshuk ◽  
Ann K. May ◽  
Leodocia M. Pope ◽  
Patricia R. Aston
Keyword(s):  
Electron Transport ◽  
Cytochrome C ◽  
Comparative Studies ◽  
Azotobacter Vinelandii ◽  
Transport Systems ◽  
Terminal Oxidase ◽  
Succinate Oxidation ◽  
State Reduction ◽  
Hydroxy Quinoline ◽  
Terminal Oxidation

A comparative study was undertaken to examine the succinate and terminal oxidase activities of the electron-transport systems of Azotobacter vinelandii and mammalian mitochondria. For succinate oxidation, both systems exhibited similar relative specificities for the electron acceptors phenazine methosulfate, O2, methylene blue, K3Fe(CN)6, nitrotetrazolium blue, 2,6-dichlorophenolindophenol (DCIP), and cytochrome c. They differed in that DCIP and cytochrome c were less active in the Azotobacter electron-transport system (R3 fraction) than in the bovine mitochondrial system. Comparative studies with known inhibitors of mammalian mitochondrial electron-transport demonstrated that the succinoxidase activity of the Azotobacter R3 fraction was, at least, 2000 times less sensitive to antimycin A, 700 times less sensitive to thenoyl-trifluoroacetone, and 30 times less sensitive to 2-n-heptyl-4-hydroxy-quinoline-N-oxide. Both systems were equally sensitive to KCN, p-chloromercuribenzoic acid, and chlorpromazine.The ability of the two systems to use tetramethyl-p-phenylenediamine (TMPD) and its derivatives as electron donors, for terminal oxidation, was also similar. Studies on steady state reduction revealed that in the Azotobacter R3 fraction, the cytochromes (a2, a1, b1, c4 + c5) and flavoprotein components were reduced substantially by succinate as well as by TMPD in the presence of ascorbate. Ultrastructure analyses of the Azotobacter R3 electron-transport fraction revealed the vesicular membranous components identified as oxidosomes according to the terminology used by DeLey and contained spherical headpiece units of 80 Å in diameter which appeared to be morphologically identical with the tripartite units or the elementary particles described by Green and associates, viz., Kopaczyk et al., and by Fernandez-Moran et al.

Recognition of structurally diverse substrates by type II 3-hydroxyacyl-CoA dehydrogenase (HADH II)/Amyloid-β binding alcohol dehydrogenase (ABAD)

2000 ◽  
Vol 303 (2) ◽  
pp. 311-327 ◽  
Author(s):  
A.J Powell ◽  
J.A Read ◽  
M.J Banfield ◽  
F Gunn-Moore ◽  
S.D Yan ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Amyloid Β ◽  
Type Ii ◽  
Hydroxyacyl Coa Dehydrogenase

Rat lung type II cell and lamellar body: elemental composition in situ

1988 ◽  
Vol 254 (5) ◽  
pp. C614-C620 ◽  
Author(s):  
R. G. Eckenhoff ◽  
A. P. Somlyo
Keyword(s):  
Elemental Composition ◽  
Lamellar Body ◽  
Cell Types ◽  
Transport Systems ◽  
Alveolar Type ◽  
Type Ii ◽  
Freeze Dried ◽  
Type Ii Cell ◽  
The Difference

We determined the in situ elemental composition of alveolar type II cells (ATII) and lamellar bodies (LB) with electronprobe microanalysis (EPMA) of freeze-dried unstained cryosections (100-200 nm) obtained from lungs frozen in anesthetized rats. Twenty-nine ATII from seven rats were subjected to EPMA. Cytoplasmic (Cyto) composition was the following (in mmol/kg dry wt, mean +/- SE, n = 30): 136 +/- 14.1 Na, 60 +/- 2.8 Mg, 549 +/- 34.8 P, 278 +/- 10.5 S, 158 +/- 7.3 Cl, 525 +/- 26.4 K, and 6.6 +/- 0.9 Ca. LB composition was the following (n = 66): 44 +/- 4.0 Na, 7.9 +/- 0.8 Mg, 1,060 +/- 25.0 P, 79 +/- 4.8 S, 64 +/- 3.6 Cl, 114 +/- 4.1 K, and 30 +/- 0.9 Ca. P and S concentrations were consistent with previous biochemical determinations of phospholipid and protein content of isolated LBs. LBs contain significantly more Ca and less Mg than Cyto. Ca correlated significantly with LB P but not S concentration, and the reported low Ca binding affinity of similar phospholipid mixtures implies a high LB free Ca concentration. Ca was significantly higher in apical and exocytotic LBs compared with those in the perinuclear region. Differences between LB and Cyto monovalent ion concentrations are not entirely due to the difference in hydration revealed by significantly lower K-Cl ratios in LBs. The relative excess of Cl and Ca in LB suggests that these ions may be distributed by active transport systems known to be present in the Golgi apparatus and in Golgi-derived organelles of other cell types.

scholarly journals Biological Electron Transport Systems

1970 ◽  
Vol 66 (3) ◽  
pp. 837-843 ◽  
Author(s):  
D. O. Cowan ◽  
G. Pasternak ◽  
F. Kaufman
Keyword(s):  
Electron Transport ◽  
Transport Systems

scholarly journals Vibrio cholerae VciB Mediates Iron Reduction

2017 ◽  
Vol 199 (12) ◽  
Author(s):  
Eric D. Peng ◽  
Shelley M. Payne
Keyword(s):  
Electron Transport ◽  
Vibrio Cholerae ◽  
Ferrous Iron ◽  
Electron Transport Chain ◽  
Iron Reduction ◽  
Iron Transport ◽  
Ferric Iron ◽  
Transport Systems ◽  
Content Type ◽  
Transport Chain

ABSTRACT Vibrio cholerae is the causative agent of the severe diarrheal disease cholera. V. cholerae thrives within the human host, where it replicates to high numbers, but it also persists within the aquatic environments of ocean and brackish water. To survive within these nutritionally diverse environments, V. cholerae must encode the necessary tools to acquire the essential nutrient iron in all forms it may encounter. A prior study of systems involved in iron transport in V. cholerae revealed the existence of vciB, which, while unable to directly transport iron, stimulates the transport of iron through ferrous (Fe2+) iron transport systems. We demonstrate here a role for VciB in V. cholerae in which VciB stimulates the reduction of Fe3+ to Fe2+, which can be subsequently transported into the cell with the ferrous iron transporter Feo. Iron reduction is independent of functional iron transport but is associated with the electron transport chain. Comparative analysis of VciB orthologs suggests a similar role for other proteins in the VciB family. Our data indicate that VciB is a dimer located in the inner membrane with three transmembrane segments and a large periplasmic loop. Directed mutagenesis of the protein reveals two highly conserved histidine residues required for function. Taken together, our results support a model whereby VciB reduces ferric iron using energy from the electron transport chain. IMPORTANCE Vibrio cholerae is a prolific human pathogen and environmental organism. The acquisition of essential nutrients such as iron is critical for replication, and V. cholerae encodes a number of mechanisms to use iron from diverse environments. Here, we describe the V. cholerae protein VciB that increases the reduction of oxidized ferric iron (Fe3+) to the ferrous form (Fe2+), thus promoting iron acquisition through ferrous iron transporters. Analysis of VciB orthologs in Burkholderia and Aeromonas spp. suggest that they have a similar activity, allowing a functional assignment for this previously uncharacterized protein family. This study builds upon our understanding of proteins known to mediate iron reduction in bacteria.

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