The organization of formate dehydrogenase in the cytoplasmic membrane of Escherichia coli.

@article{Graham1981TheOO,
  title={The organization of formate dehydrogenase in the cytoplasmic membrane of Escherichia coli.},
  author={Alexander Graham and David H. Boxer},
  journal={The Biochemical journal},
  year={1981},
  volume={195 3},
  pages={
          627-37
        }
}
The arrangement of the proton-translocating formate dehydrogenase of the anaerobic respiratory chain of Escherichia coli within the cytoplasmic membrane was examined by direct covalent modification with non-membrane-permeant reagents. Three methods were employed, lactoperoxidase-catalysed radioiodination, labelling with diazotized [125I] di-iodosulphanilic acid and labelling with diazobenzene [35S] sulphonate. All three procedures yield consistent with the view that the two larger subunits of… 

Figures and Tables from this paper

Organization of dimethyl sulfoxide reductase in the plasma membrane of Escherichia coli
TLDR
Results show that the DmsA (catalytic subunit) and DmsB are membrane-extrinsic subunits facing the cytoplasmic side of the plasma membrane.
Topological Analysis of the Aerobic Membrane-Bound Formate Dehydrogenase of Escherichia coli
TLDR
It is suggested that the alphabeta catalytic dimer is located in the cytoplasm, with a C-terminal anchor for beta protruding into the periplasm, in contrast to previously reported predictions from sequence analysis.
Identification and localization of enzymes of the fumarate reductase and nitrate respiration systems of escherichia coli by crossed immunoelectrophoresis
TLDR
Results suggest that formate dehydrogenase is a transmembrane protein; on the other hand, the results suggest that fumarate reductase, hydrogenase, glycerol-3-phosphate dehydrogensase, nitrate reduct enzyme, and ATPase are located at the inner surface of the cytoplasmic membrane.
Purification and properties of membrane-bound hydrogenase isoenzyme 1 from anaerobically grown Escherichia coli K12.
TLDR
Hydrogenase isoenzyme 1 from the membrane fraction of anaerobically grown Escherichia coli has been purified to near homogeneity and immunological analysis revealed that the polypeptides of apparent Mr 64,000, 31,000 and 29,000 are fragments of a single Polypeptide of Mr 35,000 which is present in the detergent-dispersed membranes.
The hydrogenases and formate dehydrogenases ofEscherichia coli
TLDR
The identification of the structural genes encoding the formate dehydrogenase and hydrogenase isoenzymes has enabled a detailed dissection of how their expression is coordinated to the metabolic requirement for their products, and a picture is emerging of the extremely complex and involved path of events leading to the regulated synthesis, processing and assembly of catalytically active formate dehydrationases and hydrogenases.
Isolation and characterisation of a soluble active fragment of hydrogenase isoenzyme 2 from the membranes of anaerobically grown Escherichia coli.
An active tryptic fragment of membrane-bound hydrogenase isoenzyme 2 from anaerobically grown Escherichia coli has been purified. The soluble enzyme derivative was released from the membrane fraction
Kinetic analysis of respiratory nitrate reductase from Escherichia coli K12.
TLDR
It is concluded that the holoenzyme has two independent and spatially distinct active sites, one for quinol oxidation and the other for nitrate reduction.
Behaviour of topological marker proteins targeted to the Tat protein transport pathway
TLDR
Data suggest that the Tat and Sec pathways differ in their ability to transport heterologous passenger proteins, and that caution should be observed when using subcellular reporter fusions to determine the topological organization of Tat‐dependent membrane protein complexes.
Identification and expression of the Escherichia coli fdhD and fdhE genes, which are involved in the formation of respiratory formate dehydrogenase
TLDR
Initial experiments indicate that the region between the two genes seems not to be essential to FDH-PMS activity, which might suggest the participation of fdhE in the synthesis of the selenopolypeptide of FDH -PMS.
...
...

References

Formate dehydrogenase in E. coli membrane
  • J. Biol
  • 1981