The number of accessible SH-groups in Escherichia coli membrane vesicles is increased by ATP or by formate

Biochemical and Biophysical Research Communications

Volumn 308, Issue 3, 2003, Pages 655-659

  Mnatsakanyan, Nelli ^a   Poladian, Anna ^a   Bagramyan, Karine ^a   Trchounian, Armen ^a  

^a YEREVAN STATE UNIVERSITY   (Armenia)

Author keywords

Bioenergetics; Escherichia coli; F0F1 ATPase; Fermentation; Formate; Hydrogenases; SH groups

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALANINE; CYSTEINE; DICYCLOHEXYLCARBODIIMIDE; FORMATE DEHYDROGENASE; FORMIC ACID; GLUCOSE; HYDROGENASE; N ETHYLMALEIMIDE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE INHIBITOR; SODIUM AZIDE;

ALKALINITY; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BACTERIAL GROWTH; BACTERIAL STRAIN; CONTROLLED STUDY; CULTURE MEDIUM; ENZYME ACTIVITY; ENZYME SUBUNIT; ESCHERICHIA COLI; FERMENTATION; GENE DELETION; INHIBITION KINETICS; MEMBRANE STRUCTURE; MEMBRANE VESICLE; MUTATION; NONHUMAN; OPERON; PRIORITY JOURNAL; PROTEIN DOMAIN;

ESCHERICHIA COLI;

EID: 0042665925     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)01460-8     Document Type: Article

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