Format

Send to

Choose Destination
See comment in PubMed Commons below
Biosci Rep. 2002 Jun-Aug;22(3-4):421-30.

F0 cysteine, bCys21, in the Escherichia coli ATP synthase is involved in regulation of potassium uptake and molecular hydrogen production in anaerobic conditions.

Author information

1
Department of Biophysics, Yerevan State University, 1 Alex Manougian Street, 375049 Yerevan, Armenia.

Abstract

The single cysteine in the b subunit of the membranous F0 sector and the 19 cysteines in extramembranous F1 sector of the Escherichia coli ATP synthase were replaced by alanine. When cells were grown under anaerobic conditions on glucose, the kcat for ATP hydrolysis of membrane vesicles containing the bCys21Ala mutant enzyme, but not enzymes with other cysteine replacements, was lower, while ATP-driven H+ pumping was unchanged. However, the ATP-dependent increase in the number of accessible thiol groups in membrane vesicles was negated. Furthermore, K+ uptake and molecular hydrogen production by whole cells and protoplasts was greatly decreased. These results indicate a role for the F0 subunit bCys21 in the functionality of F0F1 and coupling to other membranous activities under fermentative conditions.

PMID:
12516783
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire
    Loading ...
    Support Center