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Article

Redox regulation of CF1-ATPase involves interplay between the γ-subunit neck region and the turn region of the βDELSEED-loop.

Biochimica et biophysica acta - 1 Jan 2000

Buchert Felix, Konno Hiroki, Hisabori Toru

Abstract excerpt

The soluble F1 complex of ATP synthase (FoF1) is capable of ATP hydrolysis, accomplished by the minimum catalytic core subunits α3β3γ. A special feature of cyanobacterial F1 and chloroplast F1 (CF1) is an amino acid sequence inserted in the γ-subunit. The insertion is extended slightly into the CF1 enzyme containing two additional cysteines for regulation of ATPase activity via thiol modulation. This molecular...

Topics

Adenosine Triphosphate
Chloroplast Proton-Translocating ATPases
Chloroplasts
Cyanobacteria
Escherichia coli
Hydrolysis
Mutation
Oxidation-Reduction
Protein Conformation
Proton-Translocating ATPases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Recombinant Fusion Proteins

Spinacia oleracea

Structure-Activity Relationship

Sulfhydryl Compounds

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Identifiers

PMID: 25660164
DOI: 10.1016/j.bbabio.2015.01.013

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Redox regulation of CF1-ATPase involves interplay between the γ-subunit neck region and the turn region of the βDELSEED-loop.PMID 25660164Read ↗

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