Active Site of Mercuric Reductase Resides at the Subunit Interface and Requires Cys135 and Cys140 from One Subunit and Cys558 and Cys559 from the Adjacent Subunit: Evidence from in Vivo and in Vitro Heterodimer Formation

Biochemistry

Volumn 29, Issue 11, 1990, Pages 2703-2713

  Distefano, Mark D ^b   Moore, Melissa J ^c   Walsh, Christopher T ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

^b CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

^c MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; MERCURY (II) REDUCTASE; UNCLASSIFIED DRUG;

ARTICLE; ENZYME ACTIVE SITE; ENZYME SUBUNIT; NONHUMAN; PRIORITY JOURNAL;

BASE SEQUENCE; BINDING SITES; CATALYSIS; CYSTEINE; DNA; ERYTHROCYTES; ESCHERICHIA COLI; GENETIC COMPLEMENTATION TEST; HUMAN; MUTATION; OXIDATION-REDUCTION; OXIDOREDUCTASES; PROMOTER REGIONS (GENETICS); PROTEIN CONFORMATION; SUPPORT, U.S. GOV'T, P.H.S.;

EID: 0025271840     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi00463a013     Document Type: Article

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