Chlorite dismutases, DyPs, and EfeB: 3 microbial heme enzyme families comprise the CDE structural superfamily |
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Authors: | Goblirsch Brandon Kurker Richard C Streit Bennett R Wilmot Carrie M DuBois Jennifer L |
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Affiliation: | 1 Department of Biochemistry, Molecular Biology and Biophysics, 6-155 Jackson Hall, 321 Church Street SE, University of Minnesota, MN 55455, USA2 Department of Chemistry and Biochemistry, 251 Nieuwland Hall, University of Notre Dame, Notre Dame, IN 46556, USA |
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Abstract: | Heme proteins are extremely diverse, widespread, and versatile biocatalysts, sensors, and molecular transporters. The chlorite dismutase family of hemoproteins received its name due to the ability of the first-isolated members to detoxify anthropogenic ClO2−, a function believed to have evolved only in the last few decades. Family members have since been found in 15 bacterial and archaeal genera, suggesting ancient roots. A structure- and sequence-based examination of the family is presented, in which key sequence and structural motifs are identified, and possible functions for family proteins are proposed. Newly identified structural homologies moreover demonstrate clear connections to two other large, ancient, and functionally mysterious protein families. We propose calling them collectively the CDE superfamily of heme proteins. |
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Keywords: | heme protein bacteria peroxidase oxygen |
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