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Living species inhabiting ocean deeps must adapt to high hydrostatic pressure. This adaptation, which must enable functioning under conditions of promoted protein hydration, is especially important for proteins such as cytochromes P450 that exhibit functionally important hydrationdehydration dynamics. Here we study the interactions of substrates with cytochrome P450-SS9, a putative fatty acid hydroxylase from the piezophilic bacterium Photobacterium profundum SS9, and characterize the protein'sdoi:10.1080/08957959.2010.535208 pmid:21475616 pmcid:PMC3070315 fatcat:2k4gm5f4sjdvjceqhyfnybs3qm