ATPase activity associated with the magnesium-protoporphyrin IX chelatase enzyme of Synechocystis PCC6803: Evidence for ATP hydrolysis during Mg2+ insertion, and the MgATP-dependent interaction of the ChlI and ChlD subunits

Biochemical Journal

Volumn 339, Issue 1, 1999, Pages 127-134

  Jensen, Poul E ^a,b   Gibson, Lucien C D ^a,c   Hunter, C Neil ^a  

^a UNIVERSITY OF SHEFFIELD   (United Kingdom)

^b UNIVERSITY OF COPENHAGEN   (Denmark)

^c BEATSON INSTITUTE FOR CANCER RESEARCH   (United Kingdom)

Author keywords

ATP analogues; Chlorophyll biosynthesis; Enzyme activation; Protein protein interaction; Tetrapyrrole

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; CHLOROPHYLL; MAGNESIUM; PROTOPORPHYRIN;

ARTICLE; BIOSYNTHESIS; CHELATION; COMPLEX FORMATION; CYANOBACTERIUM; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME SUBUNIT; HYDROLYSIS; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEINS; CYANOBACTERIA; HYDROLYSIS; LYASES; MAGNESIUM; PROTEINS;

EID: 0033119836     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3390127     Document Type: Article

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