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• W2313194818 endingPage "1662" @default.
• W2313194818 startingPage "1648" @default.
• W2313194818 abstract "Catalase-peroxidases (KatGs), the only catalase-active members of their superfamily, all possess a 35-residue interhelical loop called large loop 2 (LL2). It is essential for catalase activity, but little is known about its contribution to KatG function. LL2 shows weak sequence conservation; however, its length is nearly identical across KatGs, and its apex invariably makes contact with the KatG-unique C-terminal domain. We used site-directed and deletion mutagenesis to interrogate the role of LL2 and its interaction with the C-terminal domain in KatG structure and catalysis. Single and double substitutions of the LL2 apex had little impact on the active site heme [by magnetic circular dichroism or electron paramagnetic resonance (EPR)] and activity (catalase or peroxidase). Conversely, deletion of a single amino acid from the LL2 apex reduced catalase activity by 80%. Deletion of two or more apex amino acids or all of LL2 diminished catalase activity by 300-fold. Peroxide-dependent but not electron donor-dependent kcat/KM values for deletion variant peroxidase activity were reduced 20–200-fold, and kon for cyanide binding diminished by 3 orders of magnitude. EPR spectra for deletion variants were all consistent with an increase in the level of pentacoordinate high-spin heme at the expense of hexacoordinate high-spin states. Together, these data suggest a shift in the distribution of active site waters, altering the reactivity of the ferric state, toward, among other things, compound I formation. These results identify the importance of LL2 length conservation for maintaining an intersubunit interaction that is essential for an active site water distribution that facilitates KatG catalytic activity." @default.
• W2313194818 created "2016-06-24" @default.
• W2313194818 creator A5019781120 @default.
• W2313194818 creator A5043881366 @default.
• W2313194818 creator A5046660337 @default.
• W2313194818 creator A5051793052 @default.
• W2313194818 creator A5073487526 @default.
• W2313194818 creator A5089940605 @default.
• W2313194818 date "2015-02-23" @default.
• W2313194818 modified "2023-10-07" @default.
• W2313194818 title "A Role for Catalase-Peroxidase Large Loop 2 Revealed by Deletion Mutagenesis: Control of Active Site Water and Ferric Enzyme Reactivity" @default.
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• W2313194818 doi "https://doi.org/10.1021/bi501221a" @default.
• W2313194818 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25674665" @default.
• W2313194818 hasPublicationYear "2015" @default.
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