Activation of MgADP-inactivated chloroplast F1-ATPase depends on oxyanion binding to noncatalytic sites. | Dokl Biochem Biophys;450: 123-5, 2013. | MEDLINE

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Activation of MgADP-inactivated chloroplast F1-ATPase depends on oxyanion binding to noncatalytic sites.

Malyan, A N.

Affiliation

Malyan AN; Russian Academy of Sciences, Moscow oblast, Russia.

Dokl Biochem Biophys ; 450: 123-5, 2013.

Article in En | MEDLINE | ID: mdl-23824451

Subject(s)

Adenosine Diphosphate/chemistry; Chloroplast Proton-Translocating ATPases/chemistry; Chloroplasts/enzymology; Anions/chemistry; Binding Sites; Catalytic Domain

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Adenosine Diphosphate / Chloroplasts / Chloroplast Proton-Translocating ATPases Language: En Journal: Dokl Biochem Biophys Journal subject: BIOFISICA / BIOQUIMICA Year: 2013 Document type: Article Affiliation country: Russia Country of publication: United States

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Adenosine Diphosphate / Chloroplasts / Chloroplast Proton-Translocating ATPases Language: En Journal: Dokl Biochem Biophys Journal subject: BIOFISICA / BIOQUIMICA Year: 2013 Document type: Article Affiliation country: Russia Country of publication: United States