Rational design of tertiary coordination sphere of a heme-based sensor for two-orders enhanced oxygen affinity.
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ABSTRACT: Biological O2 sensing is crucial for diverse physiological functions across all forms of life. Heme-containing proteins achieve this by binding O2 to their iron center and have been found to display O2 affinities spanning several orders of magnitude. Despite decades of investigation into the structure and function of heme-based O2 sensors, the molecular mechanisms that enable the tuning of O2 affinity to match specific physiological roles remain unclear. Here, we utilize the O2 sensing mycobacterial DosS protein as a model system to explore the role of heme iron's tertiary coordination sphere in controlling its O2 affinity. By rationally and systematically modifying the tertiary coordination sphere to promote the
SUBMITTER: Damodaran AR
PROVIDER: S-EPMC12154584 | biostudies-literature | 2025 Jul
REPOSITORIES: biostudies-literature
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