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• W2081911295 abstract "Mycobacterium tuberculosis catalase-peroxidase (Mtb KatG) is a bifunctional enzyme that possesses both catalase and peroxidase activities and is responsible for the activation of the antituberculosis drug isoniazid. Mtb KatG contains an unusual adduct in its distal heme-pocket that consists of the covalently linked Trp107, Tyr229, and Met255. The KatG(Y229F) mutant lacks this adduct and has decreased steady-state catalase activity and enhanced peroxidase activity. In order to test a potential structural role of the adduct that supports catalase activity, we have used resonance Raman spectroscopy to probe the local heme environment of KatG(Y229F). In comparison to wild-type KatG, resting KatG(Y229F) contains a significant amount of 6-coordinate, low-spin heme and a more planar heme. Resonance Raman spectroscopy of the ferrous–CO complex of KatG(Y229F) suggest a non-linear Fe–CO binding geometry that is less tilted than in wild-type KatG. These data provide evidence that the Met–Tyr–Trp adduct imparts structural stability to the active site of KatG that seems to be important for sustaining catalase activity." @default.
• W2081911295 created "2016-06-24" @default.
• W2081911295 creator A5034426393 @default.
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• W2081911295 creator A5078205705 @default.
• W2081911295 creator A5083741791 @default.
• W2081911295 date "2007-03-01" @default.
• W2081911295 modified "2023-10-17" @default.
• W2081911295 title "Modification of the active site of Mycobacterium tuberculosis KatG after disruption of the Met–Tyr–Trp cross-linked adduct" @default.
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• W2081911295 doi "https://doi.org/10.1016/j.jinorgbio.2006.11.004" @default.
• W2081911295 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1885897" @default.
• W2081911295 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17188362" @default.
• W2081911295 hasPublicationYear "2007" @default.
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