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

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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

2014

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http://europepmc.org/articles/PMC4245977?pdf=render

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Abstract

© 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,

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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

Published Web Location

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