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Article
Peer Reviewed

X-ray structure of a Hg²⁺ complex of mercuric reductase (MerA) and quantum mechanical/molecular mechanical study of Hg²⁺ transfer between the C-terminal and buried catalytic site cysteine pairs

Miller, Susan;
Lian, P;
Guo, HB;
Riccardi, D;
Dong, A;
Parks, JM;
Xu, Q;
Pai, EF;
Miller, SM;
Wei, DQ;
Smith, JC

UC San Francisco Previously Published Works (2014)

© 2014 American Chemical Society.Mercuric reductase, MerA, is a key enzyme in bacterial mercury resistance. This homodimeric enzyme captures and reduces toxic Hg2+ to Hg0, which is relatively unreactive and can exit the cell passively. Prior to reduction,

X-ray structure of a Hg2+ complex of mercuric reductase (MerA) and quantum mechanical/molecular mechanical study of Hg2+ transfer between the C-terminal and buried catalytic site cysteine pairs

X-ray structure of a Hg²⁺ complex of mercuric reductase (MerA) and quantum mechanical/molecular mechanical study of Hg²⁺ transfer between the C-terminal and buried catalytic site cysteine pairs