Disentangling Interactions of an Azole Antibiotic with a Flavohemoglobin from S. aureus

摘要

S. aureus is an opportunistic pathogen responsible for a large number of human infections that cause systemic diseases of mild to life-threatening character (1). Flavohemoglobins (Hmps) are widespread enzymes among bacteria that take part in detoxification of deleterious compounds (such as nitric oxide), imposed to the bacteria by the immune system of the host. Typically, Hmps contain three domains: C-terminal NAD- and FAD-binding domains that together constitute a ferredoxin-NADP~+ oxidoreductase-like domain, and an N-terminal globin domain, that harbors a single B-type heme inserted in a large hydrophobic pocket (1).