Modification of cysteine residues in the Chll and ChlH subunits of magnesium chelatase results in enzyme inactivation

Biochemical Journal

Volumn 352, Issue 2, 2000, Pages 435-441

  Jensen, P E ^a   Reid, J D ^a   Hunter, C N ^a  

^a UNIVERSITY OF SHEFFIELD   (United Kingdom)

Author keywords

ATPase; Chlorophyll biosynthesis; Cysteine modification; Mg2+ chelatase; Subunit interaction; Synechocystis; Tetrapyrrole

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CHLOROPHYLL; CYSTEINE; MAGNESIUM; N ETHYLMALEIMIDE; PROTOPORPHYRIN;

ARTICLE; BIOSYNTHESIS; CHELATION; CYANOBACTERIUM; ENZYME ACTIVITY; ENZYME INACTIVATION; ESCHERICHIA COLI; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN PURIFICATION;

ADENOSINE TRIPHOSPHATASES; BACTERIAL PROTEINS; CYSTEINE; DITHIOTHREITOL; ENZYME ACTIVATION; ETHYLMALEIMIDE; LYASES;

ESCHERICHIA COLI; SYNECHOCYSTIS; SYNECHOCYSTIS SP.;

EID: 0034533228     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3520435     Document Type: Article

References (22)

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