ISSN:
1573-6881
Keywords:
H+ ATPase
;
mitochondria
;
DCCD
;
binding protein
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Physics
Notes:
Conclusions Based on our present knowledge about the composition of mitochondrial F0, it is evident that its mode of interaction with F1 is more complex in comparison with bacteria and chloroplasts. As far as the H+-channel is concerned, no definite conclusion about the involvement of other subunits besides the DCCD-binding protein can be drawn at present. This holds for mitochondria as well as for chloroplasts and bacteria. Experimental evidence is accumulating in favor of the oligomeric and asymmetrical arrangement of the H+-channel. Extraction of its few polar amino acid residues by specific agents reveals the fundamental functional importance of these residues in the path of protons across the membrane. In particular, the use of DCCD was of primary importance for elucidation of the structural features underlying the protonophoric activity. It may be hoped that application of similar new approaches in combination with studies of the intact phosphorylating assembly will help us to clarify the molecular mechanism of ATP synthesis.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00744075
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