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Mutual synergy between catalase and peroxidase activities of the bifunctional enzyme KatG is facilitated by electron hole-hopping within the enzyme.
J Biol Chem. 2017 Nov 10;292(45):18408-18421. doi: 10.1074/jbc.M117.791202. Epub 2017 Sep 27.
J Biol Chem. 2017.
PMID: 28972181
Free PMC article.
Impact of distal side water and residue 315 on ligand binding to ferric Mycobacterium tuberculosis catalase-peroxidase (KatG).
Ranguelova K, Suarez J, Metlitsky L, Yu S, Brejt SZ, Brejt SZ, Zhao L, Schelvis JP, Magliozzo RS.
Ranguelova K, et al.
Biochemistry. 2008 Nov 25;47(47):12583-92. doi: 10.1021/bi801511u.
Biochemistry. 2008.
PMID: 18956888
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Hydrogen peroxide-mediated isoniazid activation catalyzed by Mycobacterium tuberculosis catalase-peroxidase (KatG) and its S315T mutant.
Zhao X, Yu H, Yu S, Wang F, Sacchettini JC, Magliozzo RS.
Zhao X, et al.
Biochemistry. 2006 Apr 4;45(13):4131-40. doi: 10.1021/bi051967o.
Biochemistry. 2006.
PMID: 16566587
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